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*** BI06 ***elNémo ID: 221206043343109505Job options:ID = 221206043343109505 JOBID = BI06 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:
HEADER BI06
HEADER TRANSFERASE/TRANSFERASE INHIBITOR 07-JUL-14 4QTB
TITLE STRUCTURE OF HUMAN ERK1 IN COMPLEX WITH SCH772984 REVEALING A NOVEL
TITLE 2 INHIBITOR-INDUCED BINDING POCKET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 3;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: MAP KINASE 3, MAPK 3, ERT2, EXTRACELLULAR SIGNAL-REGULATED
COMPND 6 KINASE 1, ERK-1, INSULIN-STIMULATED MAP2 KINASE, MAP KINASE ISOFORM
COMPND 7 P44, P44-MAPK, MICROTUBULE-ASSOCIATED PROTEIN 2 KINASE, P44-ERK1;
COMPND 8 EC: 2.7.11.24;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ERK1, MAPK3, PRKM3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 TRANSFERASE, KINASE, MAPK, SIGNALLING, INHIBITOR, ALLOSTERIC,
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM (SGC), TRANSFERASE-TRANSFERASE
KEYWDS 4 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,T.KEATES,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
AUTHOR 2 S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 2 24-SEP-14 4QTB 1 JRNL
REVDAT 1 23-JUL-14 4QTB 0
JRNL AUTH A.CHAIKUAD,E.M C TACCONI,J.ZIMMER,Y.LIANG,N.S.GRAY,
JRNL AUTH 2 M.TARSOUNAS,S.KNAPP
JRNL TITL A UNIQUE INHIBITOR BINDING SITE IN ERK1/2 IS ASSOCIATED WITH
JRNL TITL 2 SLOW BINDING KINETICS.
JRNL REF NAT.CHEM.BIOL. V. 10 853 2014
JRNL REFN ISSN 1552-4450
JRNL PMID 25195011
JRNL DOI 10.1038/NCHEMBIO.1629
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 133341
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7044
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9557
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 500
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 193
REMARK 3 SOLVENT ATOMS : 1111
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.86000
REMARK 3 B22 (A**2) : 1.25000
REMARK 3 B33 (A**2) : -0.38000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.07000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.056
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.892
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6273 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6104 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8500 ; 1.631 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14079 ; 0.789 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 767 ; 5.695 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 297 ;37.140 ;23.603
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1126 ;11.410 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;18.793 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 921 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7316 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1464 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2880 ; 0.987 ; 0.895
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2879 ; 0.973 ; 0.893
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3619 ; 1.555 ; 1.339
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3619 ; 1.555 ; 1.339
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3393 ; 1.812 ; 1.128
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3393 ; 1.812 ; 1.128
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4848 ; 2.780 ; 1.598
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8320 ; 6.252 ; 9.919
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8318 ; 6.252 ; 9.917
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 24 A 349
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8830 46.5650 57.0340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0198 T22: 0.0248
REMARK 3 T33: 0.0384 T12: 0.0037
REMARK 3 T13: -0.0033 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.1775 L22: 0.1231
REMARK 3 L33: 0.2187 L12: -0.0042
REMARK 3 L13: -0.0332 L23: -0.0492
REMARK 3 S TENSOR
REMARK 3 S11: -0.0111 S12: 0.0028 S13: -0.0202
REMARK 3 S21: 0.0009 S22: 0.0165 S23: 0.0054
REMARK 3 S31: -0.0125 S32: -0.0028 S33: -0.0054
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 350 A 374
REMARK 3 ORIGIN FOR THE GROUP (A): 54.2390 50.0410 49.5610
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: 0.0367
REMARK 3 T33: 0.0759 T12: -0.0077
REMARK 3 T13: 0.0032 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.3376 L22: 0.7579
REMARK 3 L33: 3.3625 L12: 0.3773
REMARK 3 L13: 0.8165 L23: 0.5347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0505 S12: -0.0275 S13: -0.0326
REMARK 3 S21: 0.0227 S22: -0.0423 S23: -0.1508
REMARK 3 S31: 0.0679 S32: -0.0520 S33: -0.0081
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 27 B 349
REMARK 3 ORIGIN FOR THE GROUP (A): 56.5980 30.8560 90.6400
REMARK 3 T TENSOR
REMARK 3 T11: 0.0230 T22: 0.0167
REMARK 3 T33: 0.0398 T12: 0.0061
REMARK 3 T13: 0.0025 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.3377 L22: 0.0498
REMARK 3 L33: 0.2393 L12: 0.0235
REMARK 3 L13: 0.0901 L23: 0.0445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.0095 S13: 0.0237
REMARK 3 S21: -0.0069 S22: 0.0105 S23: -0.0011
REMARK 3 S31: -0.0074 S32: 0.0058 S33: 0.0008
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 350 B 374
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8320 27.5070 81.8550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0215 T22: 0.0344
REMARK 3 T33: 0.0597 T12: -0.0069
REMARK 3 T13: 0.0051 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.9390 L22: 0.7833
REMARK 3 L33: 3.5242 L12: 0.5810
REMARK 3 L13: -1.3860 L23: -0.4425
REMARK 3 S TENSOR
REMARK 3 S11: 0.0624 S12: -0.0958 S13: 0.0274
REMARK 3 S21: 0.0276 S22: -0.0637 S23: 0.1220
REMARK 3 S31: -0.0583 S32: 0.1075 S33: 0.0013
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4QTB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-14.
REMARK 100 THE RCSB ID CODE IS RCSB086486.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91997
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH MIRROR
REMARK 200 PAIR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140385
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 38.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.61800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2ZOQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 33% PEG4000, 0.1 M TRIS PH 8.0 AND 0.2
REMARK 280 M LITHIUM SULPHATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 47.00500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 GLN A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 12
REMARK 465 GLU A 13
REMARK 465 PRO A 14
REMARK 465 ARG A 15
REMARK 465 ARG A 16
REMARK 465 THR A 17
REMARK 465 GLU A 18
REMARK 465 GLY A 19
REMARK 465 VAL A 20
REMARK 465 GLY A 21
REMARK 465 PRO A 22
REMARK 465 GLY A 23
REMARK 465 VAL A 375
REMARK 465 LEU A 376
REMARK 465 GLU A 377
REMARK 465 ALA A 378
REMARK 465 PRO A 379
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 GLN B 7
REMARK 465 GLY B 8
REMARK 465 GLY B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 GLY B 12
REMARK 465 GLU B 13
REMARK 465 PRO B 14
REMARK 465 ARG B 15
REMARK 465 ARG B 16
REMARK 465 THR B 17
REMARK 465 GLU B 18
REMARK 465 GLY B 19
REMARK 465 VAL B 20
REMARK 465 GLY B 21
REMARK 465 PRO B 22
REMARK 465 GLY B 23
REMARK 465 VAL B 24
REMARK 465 PRO B 25
REMARK 465 GLY B 26
REMARK 465 VAL B 375
REMARK 465 LEU B 376
REMARK 465 GLU B 377
REMARK 465 ALA B 378
REMARK 465 PRO B 379
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU B 27 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 358 O HOH A 1066 2.06
REMARK 500 O HOH A 955 O HOH A 956 2.10
REMARK 500 OE1 GLU A 267 O HOH A 993 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 322 CD GLU A 322 OE1 0.083
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 141 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 152 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 166 38.56 -147.99
REMARK 500 ASP A 184 87.31 72.12
REMARK 500 ASN A 218 15.77 -163.22
REMARK 500 LEU A 311 46.49 -103.64
REMARK 500 ASP A 335 89.71 -160.81
REMARK 500 ASP B 166 41.62 -152.18
REMARK 500 ASP B 184 86.99 76.01
REMARK 500 ASN B 218 13.44 -161.99
REMARK 500 LEU B 311 35.83 -96.46
REMARK 500 ASP B 335 89.00 -161.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 762 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH A 851 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A1071 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH B 912 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH B 938 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH B 952 DISTANCE = 5.74 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38Z A 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 38Z B 412
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QTA RELATED DB: PDB
REMARK 900 RELATED ID: 4QTC RELATED DB: PDB
REMARK 900 RELATED ID: 4QTD RELATED DB: PDB
REMARK 900 RELATED ID: 4QTE RELATED DB: PDB
DBREF 4QTB A 1 379 UNP P27361 MK03_HUMAN 1 379
DBREF 4QTB B 1 379 UNP P27361 MK03_HUMAN 1 379
SEQADV 4QTB SER A 0 UNP P27361 EXPRESSION TAG
SEQADV 4QTB SER B 0 UNP P27361 EXPRESSION TAG
SEQRES 1 A 380 SER MET ALA ALA ALA ALA ALA GLN GLY GLY GLY GLY GLY
SEQRES 2 A 380 GLU PRO ARG ARG THR GLU GLY VAL GLY PRO GLY VAL PRO
SEQRES 3 A 380 GLY GLU VAL GLU MET VAL LYS GLY GLN PRO PHE ASP VAL
SEQRES 4 A 380 GLY PRO ARG TYR THR GLN LEU GLN TYR ILE GLY GLU GLY
SEQRES 5 A 380 ALA TYR GLY MET VAL SER SER ALA TYR ASP HIS VAL ARG
SEQRES 6 A 380 LYS THR ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU
SEQRES 7 A 380 HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE GLN
SEQRES 8 A 380 ILE LEU LEU ARG PHE ARG HIS GLU ASN VAL ILE GLY ILE
SEQRES 9 A 380 ARG ASP ILE LEU ARG ALA SER THR LEU GLU ALA MET ARG
SEQRES 10 A 380 ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU
SEQRES 11 A 380 TYR LYS LEU LEU LYS SER GLN GLN LEU SER ASN ASP HIS
SEQRES 12 A 380 ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS
SEQRES 13 A 380 TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS
SEQRES 14 A 380 PRO SER ASN LEU LEU ILE ASN THR THR CYS ASP LEU LYS
SEQRES 15 A 380 ILE CYS ASP PHE GLY LEU ALA ARG ILE ALA ASP PRO GLU
SEQRES 16 A 380 HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR
SEQRES 17 A 380 ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS
SEQRES 18 A 380 GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS
SEQRES 19 A 380 ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO
SEQRES 20 A 380 GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY
SEQRES 21 A 380 ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE
SEQRES 22 A 380 ILE ASN MET LYS ALA ARG ASN TYR LEU GLN SER LEU PRO
SEQRES 23 A 380 SER LYS THR LYS VAL ALA TRP ALA LYS LEU PHE PRO LYS
SEQRES 24 A 380 SER ASP SER LYS ALA LEU ASP LEU LEU ASP ARG MET LEU
SEQRES 25 A 380 THR PHE ASN PRO ASN LYS ARG ILE THR VAL GLU GLU ALA
SEQRES 26 A 380 LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO THR
SEQRES 27 A 380 ASP GLU PRO VAL ALA GLU GLU PRO PHE THR PHE ALA MET
SEQRES 28 A 380 GLU LEU ASP ASP LEU PRO LYS GLU ARG LEU LYS GLU LEU
SEQRES 29 A 380 ILE PHE GLN GLU THR ALA ARG PHE GLN PRO GLY VAL LEU
SEQRES 30 A 380 GLU ALA PRO
SEQRES 1 B 380 SER MET ALA ALA ALA ALA ALA GLN GLY GLY GLY GLY GLY
SEQRES 2 B 380 GLU PRO ARG ARG THR GLU GLY VAL GLY PRO GLY VAL PRO
SEQRES 3 B 380 GLY GLU VAL GLU MET VAL LYS GLY GLN PRO PHE ASP VAL
SEQRES 4 B 380 GLY PRO ARG TYR THR GLN LEU GLN TYR ILE GLY GLU GLY
SEQRES 5 B 380 ALA TYR GLY MET VAL SER SER ALA TYR ASP HIS VAL ARG
SEQRES 6 B 380 LYS THR ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU
SEQRES 7 B 380 HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE GLN
SEQRES 8 B 380 ILE LEU LEU ARG PHE ARG HIS GLU ASN VAL ILE GLY ILE
SEQRES 9 B 380 ARG ASP ILE LEU ARG ALA SER THR LEU GLU ALA MET ARG
SEQRES 10 B 380 ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU
SEQRES 11 B 380 TYR LYS LEU LEU LYS SER GLN GLN LEU SER ASN ASP HIS
SEQRES 12 B 380 ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS
SEQRES 13 B 380 TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS
SEQRES 14 B 380 PRO SER ASN LEU LEU ILE ASN THR THR CYS ASP LEU LYS
SEQRES 15 B 380 ILE CYS ASP PHE GLY LEU ALA ARG ILE ALA ASP PRO GLU
SEQRES 16 B 380 HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR
SEQRES 17 B 380 ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS
SEQRES 18 B 380 GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS
SEQRES 19 B 380 ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO
SEQRES 20 B 380 GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY
SEQRES 21 B 380 ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE
SEQRES 22 B 380 ILE ASN MET LYS ALA ARG ASN TYR LEU GLN SER LEU PRO
SEQRES 23 B 380 SER LYS THR LYS VAL ALA TRP ALA LYS LEU PHE PRO LYS
SEQRES 24 B 380 SER ASP SER LYS ALA LEU ASP LEU LEU ASP ARG MET LEU
SEQRES 25 B 380 THR PHE ASN PRO ASN LYS ARG ILE THR VAL GLU GLU ALA
SEQRES 26 B 380 LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO THR
SEQRES 27 B 380 ASP GLU PRO VAL ALA GLU GLU PRO PHE THR PHE ALA MET
SEQRES 28 B 380 GLU LEU ASP ASP LEU PRO LYS GLU ARG LEU LYS GLU LEU
SEQRES 29 B 380 ILE PHE GLN GLU THR ALA ARG PHE GLN PRO GLY VAL LEU
SEQRES 30 B 380 GLU ALA PRO
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 8
HET EDO A 407 8
HET EDO A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET EDO A 411 4
HET EDO A 412 4
HET EDO A 413 4
HET DMS A 414 4
HET DMS A 415 4
HET CL A 416 1
HET SO4 A 417 5
HET 38Z A 418 44
HET EDO B 401 8
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HET EDO B 405 4
HET EDO B 406 4
HET EDO B 407 4
HET DMS B 408 4
HET CL B 409 1
HET CL B 410 1
HET SO4 B 411 5
HET 38Z B 412 44
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM 38Z (3R)-1-(2-OXO-2-{4-[4-(PYRIMIDIN-2-YL)PHENYL]PIPERAZIN-
HETNAM 2 38Z 1-YL}ETHYL)-N-[3-(PYRIDIN-4-YL)-2H-INDAZOL-5-
HETNAM 3 38Z YL]PYRROLIDINE-3-CARBOXAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 20(C2 H6 O2)
FORMUL 16 DMS 3(C2 H6 O S)
FORMUL 18 CL 3(CL 1-)
FORMUL 19 SO4 2(O4 S 2-)
FORMUL 20 38Z 2(C33 H33 N9 O2)
FORMUL 33 HOH *1111(H2 O)
HELIX 1 1 HIS A 78 PHE A 95 1 18
HELIX 2 2 LEU A 129 GLN A 136 1 8
HELIX 3 3 SER A 139 ALA A 160 1 22
HELIX 4 4 LYS A 168 SER A 170 5 3
HELIX 5 5 ASP A 192 ASP A 196 5 5
HELIX 6 6 THR A 207 ARG A 211 5 5
HELIX 7 7 ALA A 212 MET A 216 5 5
HELIX 8 8 LYS A 224 ASN A 241 1 18
HELIX 9 9 HIS A 249 GLY A 262 1 14
HELIX 10 10 SER A 265 ASN A 270 1 6
HELIX 11 11 ASN A 274 SER A 283 1 10
HELIX 12 12 ALA A 291 PHE A 296 1 6
HELIX 13 13 ASP A 300 LEU A 311 1 12
HELIX 14 14 ASN A 314 ARG A 318 5 5
HELIX 15 15 THR A 320 ALA A 326 1 7
HELIX 16 16 HIS A 327 GLU A 331 5 5
HELIX 17 17 ASP A 335 GLU A 339 5 5
HELIX 18 18 ALA A 349 LEU A 355 5 7
HELIX 19 19 PRO A 356 ALA A 369 1 14
HELIX 20 20 ARG A 370 GLN A 372 5 3
HELIX 21 21 HIS B 78 PHE B 95 1 18
HELIX 22 22 LEU B 129 GLN B 136 1 8
HELIX 23 23 SER B 139 ALA B 160 1 22
HELIX 24 24 LYS B 168 SER B 170 5 3
HELIX 25 25 ASP B 192 ASP B 196 5 5
HELIX 26 26 THR B 207 ARG B 211 5 5
HELIX 27 27 ALA B 212 MET B 216 5 5
HELIX 28 28 LYS B 224 ASN B 241 1 18
HELIX 29 29 HIS B 249 GLY B 262 1 14
HELIX 30 30 SER B 265 ASN B 270 1 6
HELIX 31 31 ASN B 274 SER B 283 1 10
HELIX 32 32 ALA B 291 PHE B 296 1 6
HELIX 33 33 ASP B 300 LEU B 311 1 12
HELIX 34 34 THR B 320 ALA B 326 1 7
HELIX 35 35 HIS B 327 GLU B 331 5 5
HELIX 36 36 ASP B 335 GLU B 339 5 5
HELIX 37 37 ALA B 349 LEU B 355 5 7
HELIX 38 38 PRO B 356 ALA B 369 1 14
HELIX 39 39 ARG B 370 GLN B 372 5 3
SHEET 1 A 2 GLU A 29 VAL A 31 0
SHEET 2 A 2 GLN A 34 PHE A 36 -1 O PHE A 36 N GLU A 29
SHEET 1 B 5 TYR A 42 GLY A 51 0
SHEET 2 B 5 GLY A 54 ASP A 61 -1 O TYR A 60 N THR A 43
SHEET 3 B 5 THR A 66 ILE A 73 -1 O THR A 66 N ASP A 61
SHEET 4 B 5 VAL A 118 GLN A 122 -1 O GLN A 122 N ALA A 69
SHEET 5 B 5 ASP A 105 LEU A 107 -1 N ASP A 105 O VAL A 121
SHEET 1 C 3 THR A 127 ASP A 128 0
SHEET 2 C 3 LEU A 172 ILE A 174 -1 O ILE A 174 N THR A 127
SHEET 3 C 3 LEU A 180 ILE A 182 -1 O LYS A 181 N LEU A 173
SHEET 1 D 2 VAL A 162 LEU A 163 0
SHEET 2 D 2 ARG A 189 ILE A 190 -1 O ARG A 189 N LEU A 163
SHEET 1 E 2 GLU B 29 VAL B 31 0
SHEET 2 E 2 GLN B 34 PHE B 36 -1 O GLN B 34 N VAL B 31
SHEET 1 F 5 TYR B 42 GLY B 51 0
SHEET 2 F 5 GLY B 54 ASP B 61 -1 O TYR B 60 N THR B 43
SHEET 3 F 5 THR B 66 ILE B 73 -1 O ILE B 70 N SER B 57
SHEET 4 F 5 VAL B 118 GLN B 122 -1 O GLN B 122 N ALA B 69
SHEET 5 F 5 ASP B 105 LEU B 107 -1 N ASP B 105 O VAL B 121
SHEET 1 G 3 THR B 127 ASP B 128 0
SHEET 2 G 3 LEU B 172 ILE B 174 -1 O ILE B 174 N THR B 127
SHEET 3 G 3 LEU B 180 ILE B 182 -1 O LYS B 181 N LEU B 173
SHEET 1 H 2 VAL B 162 LEU B 163 0
SHEET 2 H 2 ARG B 189 ILE B 190 -1 O ARG B 189 N LEU B 163
CISPEP 1 GLY A 39 PRO A 40 0 6.07
CISPEP 2 GLN A 372 PRO A 373 0 -5.36
CISPEP 3 GLY B 39 PRO B 40 0 5.17
CISPEP 4 GLN B 372 PRO B 373 0 -5.80
SITE 1 AC1 3 ASP A 37 LEU A 107 HOH A 635
SITE 1 AC2 6 GLU A 98 ASN A 99 GLN A 149 ARG A 152
SITE 2 AC2 6 ASP A 179 HOH A 576
SITE 1 AC3 4 LEU A 201 GLU A 203 TYR A 250 HOH A1051
SITE 1 AC4 8 ARG A 84 ARG A 87 GLY A 186 LEU A 187
SITE 2 AC4 8 ALA A 188 ARG A 189 HOH A 704 HOH A 926
SITE 1 AC5 4 TYR A 130 SER A 170 EDO A 413 HOH A 733
SITE 1 AC6 7 ILE A 190 ALA A 191 THR A 347 PHE A 348
SITE 2 AC6 7 ALA A 349 DMS A 415 HOH A 976
SITE 1 AC7 7 ASP A 141 TYR A 145 TYR A 333 HOH A 974
SITE 2 AC7 7 LYS B 289 VAL B 290 ALA B 291
SITE 1 AC8 4 SER A 263 PRO A 285 HOH A 595 HOH A1008
SITE 1 AC9 6 SER A 263 LEU A 281 GLN A 282 LEU A 284
SITE 2 AC9 6 SER A 286 HOH A 578
SITE 1 BC1 1 GLU A 323
SITE 1 BC2 5 PRO A 40 ARG A 41 HIS A 62 VAL A 63
SITE 2 BC2 5 HOH A 908
SITE 1 BC3 4 LYS A 65 LEU A 201 TYR A 280 HOH A 911
SITE 1 BC4 5 ASP A 128 TYR A 130 EDO A 405 HOH A 685
SITE 2 BC4 5 HOH A1026
SITE 1 BC5 4 LEU A 239 SER A 299 HOH A 541 HOH A 731
SITE 1 BC6 7 ARG A 189 ILE A 190 ASP A 192 PHE A 348
SITE 2 BC6 7 MET A 350 EDO A 406 HOH A 574
SITE 1 BC7 5 HIS A 197 ASN A 218 ILE A 273 ASN A 274
SITE 2 BC7 5 ARG B 94
SITE 1 BC8 8 ARG A 208 ARG A 211 TYR A 250 HOH A 936
SITE 2 BC8 8 HOH A 942 HOH A1018 HOH A1019 HOH A1051
SITE 1 BC9 21 ALA A 52 TYR A 53 ALA A 69 LYS A 71
SITE 2 BC9 21 ILE A 73 TYR A 81 ARG A 84 THR A 85
SITE 3 BC9 21 GLU A 88 GLN A 122 ASP A 123 MET A 125
SITE 4 BC9 21 GLU A 126 THR A 127 LYS A 131 LEU A 173
SITE 5 BC9 21 ASP A 184 GLY A 186 HOH A 517 HOH A 856
SITE 6 BC9 21 HOH A1017
SITE 1 CC1 6 ARG B 189 ILE B 190 ASP B 192 TYR B 222
SITE 2 CC1 6 PHE B 348 HOH B 847
SITE 1 CC2 8 ARG B 84 ARG B 87 GLY B 186 LEU B 187
SITE 2 CC2 8 ALA B 188 ARG B 189 HOH B 848 HOH B 981
SITE 1 CC3 3 TYR B 130 SER B 170 HOH B 751
SITE 1 CC4 5 ASP B 37 ALA B 109 HOH B 738 HOH B 802
SITE 2 CC4 5 HOH B 807
SITE 1 CC5 3 SER B 263 PRO B 285 HOH B 634
SITE 1 CC6 2 LEU B 201 GLU B 203
SITE 1 CC7 7 LEU B 133 LYS B 134 GLU B 237 ASN B 241
SITE 2 CC7 7 ARG B 242 PRO B 243 HOH B 931
SITE 1 CC8 6 LEU B 239 LYS B 298 SER B 299 HOH B 610
SITE 2 CC8 6 HOH B 665 HOH B 996
SITE 1 CC9 5 ARG A 94 HIS B 197 ASN B 218 ILE B 273
SITE 2 CC9 5 ASN B 274
SITE 1 DC1 2 HIS B 78 GLN B 79
SITE 1 DC2 7 ARG B 208 ARG B 211 TYR B 250 HOH B 521
SITE 2 DC2 7 HOH B 592 HOH B 760 HOH B 960
SITE 1 DC3 22 ALA B 52 TYR B 53 ALA B 69 LYS B 71
SITE 2 DC3 22 ILE B 73 TYR B 81 ARG B 84 THR B 85
SITE 3 DC3 22 GLU B 88 GLN B 122 ASP B 123 MET B 125
SITE 4 DC3 22 GLU B 126 THR B 127 LYS B 131 LEU B 173
SITE 5 DC3 22 ASP B 184 GLY B 186 HOH B 541 HOH B 578
SITE 6 DC3 22 HOH B 971 HOH B 972
CRYST1 61.980 94.010 65.360 90.00 91.71 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016134 0.000000 0.000482 0.00000
SCALE2 0.000000 0.010637 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015307 0.00000
ATOM 1 N VAL A 24 38.456 71.796 27.369 1.00 45.99 N
ANISOU 1 N VAL A 24 5945 5852 5675 -102 35 235 N
ATOM 2 CA VAL A 24 39.876 72.055 26.951 1.00 45.57 C
ANISOU 2 CA VAL A 24 5892 5802 5619 -123 47 238 C
ATOM 3 C VAL A 24 40.560 70.696 26.773 1.00 45.60 C
ANISOU 3 C VAL A 24 5877 5832 5617 -130 48 215 C
ATOM 4 O VAL A 24 40.551 69.872 27.697 1.00 43.80 O
ANISOU 4 O VAL A 24 5640 5602 5400 -128 44 194 O
ATOM 5 CB VAL A 24 40.658 72.933 27.994 1.00 47.27 C
ANISOU 5 CB VAL A 24 6117 5987 5856 -137 53 237 C
ATOM 6 CG1 VAL A 24 42.030 73.358 27.453 1.00 46.48 C
ANISOU 6 CG1 VAL A 24 6018 5891 5753 -159 65 245 C
ATOM 7 CG2 VAL A 24 39.857 74.174 28.374 1.00 48.59 C
ANISOU 7 CG2 VAL A 24 6305 6125 6033 -127 51 255 C
ATOM 8 N PRO A 25 41.137 70.441 25.582 1.00 46.28 N
ANISOU 8 N PRO A 25 5957 5942 5684 -138 55 221 N
ATOM 9 CA PRO A 25 41.739 69.110 25.320 1.00 44.50 C
ANISOU 9 CA PRO A 25 5715 5741 5450 -142 58 199 C
ATOM 10 C PRO A 25 42.903 68.796 26.258 1.00 38.41 C
ANISOU 10 C PRO A 25 4935 4962 4696 -155 63 183 C
ATOM 11 O PRO A 25 43.768 69.654 26.460 1.00 36.31 O
ANISOU 11 O PRO A 25 4674 4683 4438 -170 71 193 O
ATOM 12 CB PRO A 25 42.246 69.209 23.866 1.00 47.12 C
ANISOU 12 CB PRO A 25 6046 6098 5759 -149 67 212 C
ATOM 13 CG PRO A 25 42.138 70.645 23.463 1.00 48.75 C
ANISOU 13 CG PRO A 25 6268 6290 5963 -152 71 241 C
ATOM 14 CD PRO A 25 41.501 71.448 24.562 1.00 48.53 C
ANISOU 14 CD PRO A 25 6252 6229 5956 -146 64 246 C
ATOM 15 N GLY A 26 42.902 67.592 26.849 1.00 34.62 N
ANISOU 15 N GLY A 26 4442 4489 4221 -151 59 159 N
ATOM 16 CA GLY A 26 43.976 67.159 27.761 1.00 30.63 C
ANISOU 16 CA GLY A 26 3928 3980 3732 -161 63 143 C
ATOM 17 C GLY A 26 43.881 67.776 29.157 1.00 26.84 C
ANISOU 17 C GLY A 26 3454 3470 3274 -163 58 141 C
ATOM 18 O GLY A 26 44.818 67.704 29.940 1.00 25.63 O
ANISOU 18 O GLY A 26 3295 3311 3133 -174 61 132 O
ATOM 19 N GLU A 27 42.749 68.416 29.441 1.00 24.16 N
ANISOU 19 N GLU A 27 3128 3114 2938 -151 50 150 N
ATOM 20 CA GLU A 27 42.565 69.109 30.691 1.00 24.28 C
ANISOU 20 CA GLU A 27 3152 3101 2972 -152 46 150 C
ATOM 21 C GLU A 27 42.627 68.096 31.841 1.00 20.43 C
ANISOU 21 C GLU A 27 2653 2612 2496 -148 41 126 C
ATOM 22 O GLU A 27 42.289 66.923 31.708 1.00 22.32 O
ANISOU 22 O GLU A 27 2881 2869 2731 -139 37 113 O
ATOM 23 CB GLU A 27 41.214 69.824 30.724 1.00 27.61 C
ANISOU 23 CB GLU A 27 3589 3508 3394 -136 40 163 C
ATOM 24 CG GLU A 27 40.038 68.847 30.640 1.00 31.66 C
ANISOU 24 CG GLU A 27 4094 4035 3901 -117 30 154 C
ATOM 25 CD GLU A 27 38.673 69.500 30.739 1.00 36.52 C
ANISOU 25 CD GLU A 27 4721 4638 4517 -100 23 167 C
ATOM 26 OE1 GLU A 27 38.587 70.694 31.120 1.00 40.99 O
ANISOU 26 OE1 GLU A 27 5303 5180 5093 -101 25 180 O
ATOM 27 OE2 GLU A 27 37.677 68.787 30.453 1.00 43.04 O
ANISOU 27 OE2 GLU A 27 5540 5478 5336 -87 15 163 O
ATOM 28 N VAL A 28 43.043 68.576 32.985 1.00 16.77 N
ANISOU 28 N VAL A 28 2194 2128 2049 -155 40 122 N
ATOM 29 CA VAL A 28 42.851 67.812 34.207 1.00 14.69 C
ANISOU 29 CA VAL A 28 1924 1860 1798 -149 33 103 C
ATOM 30 C VAL A 28 41.469 68.184 34.718 1.00 14.15 C
ANISOU 30 C VAL A 28 1867 1776 1734 -132 26 107 C
ATOM 31 O VAL A 28 41.207 69.347 35.088 1.00 14.30 O
ANISOU 31 O VAL A 28 1902 1772 1759 -132 26 118 O
ATOM 32 CB VAL A 28 43.932 68.123 35.242 1.00 14.25 C
ANISOU 32 CB VAL A 28 1867 1793 1757 -164 36 96 C
ATOM 33 CG1 VAL A 28 43.631 67.460 36.572 1.00 14.36 C
ANISOU 33 CG1 VAL A 28 1875 1799 1781 -156 28 78 C
ATOM 34 CG2 VAL A 28 45.300 67.716 34.731 1.00 14.48 C
ANISOU 34 CG2 VAL A 28 1882 1840 1781 -180 44 93 C
ATOM 35 N GLU A 29 40.559 67.209 34.752 1.00 13.74 N
ANISOU 35 N GLU A 29 1808 1735 1680 -117 19 98 N
ATOM 36 CA GLU A 29 39.213 67.453 35.243 1.00 13.52 C
ANISOU 36 CA GLU A 29 1787 1695 1656 -100 11 101 C
ATOM 37 C GLU A 29 39.156 67.596 36.739 1.00 13.87 C
ANISOU 37 C GLU A 29 1836 1720 1716 -98 8 91 C
ATOM 38 O GLU A 29 39.872 66.931 37.480 1.00 13.40 O
ANISOU 38 O GLU A 29 1767 1662 1663 -104 8 76 O
ATOM 39 CB GLU A 29 38.257 66.322 34.803 1.00 13.96 C
ANISOU 39 CB GLU A 29 1832 1770 1703 -86 5 95 C
ATOM 40 CG GLU A 29 38.132 66.155 33.281 1.00 14.94 C
ANISOU 40 CG GLU A 29 1953 1915 1808 -87 6 104 C
ATOM 41 CD GLU A 29 36.947 65.303 32.819 1.00 16.08 C
ANISOU 41 CD GLU A 29 2089 2076 1944 -73 -2 101 C
ATOM 42 OE1 GLU A 29 35.955 65.188 33.528 1.00 16.23 O
ANISOU 42 OE1 GLU A 29 2109 2087 1971 -61 -9 98 O
ATOM 43 OE2 GLU A 29 37.037 64.783 31.690 1.00 21.01 O
ANISOU 43 OE2 GLU A 29 2708 2721 2553 -75 -1 101 O
ATOM 44 N MET A 30 38.289 68.484 37.180 1.00 12.90 N
ANISOU 44 N MET A 30 1727 1578 1598 -87 6 100 N
ATOM 45 CA MET A 30 38.162 68.817 38.579 1.00 13.63 C
ANISOU 45 CA MET A 30 1826 1649 1703 -85 4 92 C
ATOM 46 C MET A 30 36.885 68.241 39.083 1.00 13.74 C
ANISOU 46 C MET A 30 1836 1666 1720 -65 -2 88 C
ATOM 47 O MET A 30 35.862 68.347 38.410 1.00 15.18 O
ANISOU 47 O MET A 30 2019 1853 1895 -52 -5 99 O
ATOM 48 CB MET A 30 38.141 70.344 38.800 1.00 14.67 C
ANISOU 48 CB MET A 30 1980 1755 1841 -87 8 105 C
ATOM 49 CG MET A 30 39.359 71.071 38.275 1.00 15.03 C
ANISOU 49 CG MET A 30 2031 1796 1885 -108 16 112 C
ATOM 50 SD MET A 30 40.829 70.581 39.225 1.00 15.54 S
ANISOU 50 SD MET A 30 2084 1861 1957 -129 16 93 S
ATOM 51 CE MET A 30 42.116 70.987 38.031 1.00 17.20 C
ANISOU 51 CE MET A 30 2292 2082 2160 -151 25 105 C
ATOM 52 N VAL A 31 36.939 67.700 40.281 1.00 12.77 N
ANISOU 52 N VAL A 31 1709 1538 1606 -63 -5 72 N
ATOM 53 CA VAL A 31 35.754 67.219 41.006 1.00 13.59 C
ANISOU 53 CA VAL A 31 1809 1641 1714 -46 -11 68 C
ATOM 54 C VAL A 31 35.723 67.908 42.333 1.00 13.77 C
ANISOU 54 C VAL A 31 1843 1640 1747 -43 -10 63 C
ATOM 55 O VAL A 31 36.596 67.692 43.189 1.00 14.37 O
ANISOU 55 O VAL A 31 1917 1712 1828 -54 -9 51 O
ATOM 56 CB VAL A 31 35.784 65.699 41.181 1.00 14.44 C
ANISOU 56 CB VAL A 31 1898 1767 1821 -45 -15 53 C
ATOM 57 CG1 VAL A 31 34.473 65.241 41.830 1.00 15.12 C
ANISOU 57 CG1 VAL A 31 1980 1854 1911 -27 -20 51 C
ATOM 58 CG2 VAL A 31 35.964 64.996 39.831 1.00 16.02 C
ANISOU 58 CG2 VAL A 31 2087 1989 2010 -50 -15 55 C
ATOM 59 N LYS A 32 34.752 68.811 42.498 1.00 13.74 N
ANISOU 59 N LYS A 32 1854 1622 1745 -29 -9 74 N
ATOM 60 CA LYS A 32 34.606 69.533 43.711 1.00 15.31 C
ANISOU 60 CA LYS A 32 2067 1798 1953 -25 -7 70 C
ATOM 61 C LYS A 32 35.968 70.152 44.155 1.00 15.86 C
ANISOU 61 C LYS A 32 2146 1854 2027 -46 -4 63 C
ATOM 62 O LYS A 32 36.416 70.042 45.307 1.00 16.98 O
ANISOU 62 O LYS A 32 2290 1989 2175 -51 -5 50 O
ATOM 63 CB LYS A 32 33.949 68.603 44.766 1.00 15.94 C
ANISOU 63 CB LYS A 32 2136 1883 2036 -13 -12 57 C
ATOM 64 CG LYS A 32 33.095 69.352 45.746 1.00 15.88 C
ANISOU 64 CG LYS A 32 2142 1856 2034 2 -10 58 C
ATOM 65 CD LYS A 32 32.617 68.500 46.878 1.00 14.59 C
ANISOU 65 CD LYS A 32 1970 1699 1876 11 -13 46 C
ATOM 66 CE LYS A 32 32.127 69.416 47.996 1.00 15.71 C
ANISOU 66 CE LYS A 32 2129 1818 2022 23 -9 45 C
ATOM 67 NZ LYS A 32 31.653 68.637 49.158 1.00 14.66 N
ANISOU 67 NZ LYS A 32 1988 1691 1893 32 -11 33 N
ATOM 68 N GLY A 33 36.618 70.814 43.198 1.00 15.33 N
ANISOU 68 N GLY A 33 2085 1784 1956 -58 0 74 N
ATOM 69 CA GLY A 33 37.903 71.506 43.459 1.00 16.73 C
ANISOU 69 CA GLY A 33 2270 1948 2136 -81 4 71 C
ATOM 70 C GLY A 33 39.119 70.601 43.565 1.00 16.14 C
ANISOU 70 C GLY A 33 2179 1892 2062 -98 2 58 C
ATOM 71 O GLY A 33 40.217 71.070 43.860 1.00 16.81 O
ANISOU 71 O GLY A 33 2267 1969 2150 -117 4 54 O
ATOM 72 N GLN A 34 38.951 69.294 43.360 1.00 14.62 N
ANISOU 72 N GLN A 34 1967 1722 1865 -92 -1 51 N
ATOM 73 CA AGLN A 34 40.055 68.304 43.465 0.50 15.09 C
ANISOU 73 CA AGLN A 34 2009 1800 1925 -105 -2 40 C
ATOM 74 CA BGLN A 34 40.077 68.413 43.432 0.50 14.77 C
ANISOU 74 CA BGLN A 34 1969 1757 1884 -106 -2 40 C
ATOM 75 C GLN A 34 40.400 67.831 42.058 1.00 13.59 C
ANISOU 75 C GLN A 34 1808 1630 1727 -110 1 46 C
ATOM 76 O GLN A 34 39.549 67.302 41.351 1.00 12.72 O
ANISOU 76 O GLN A 34 1692 1531 1609 -97 -1 51 O
ATOM 77 CB AGLN A 34 39.664 67.050 44.292 0.50 16.52 C
ANISOU 77 CB AGLN A 34 2176 1991 2109 -94 -8 26 C
ATOM 78 CB BGLN A 34 39.840 67.378 44.502 0.50 15.96 C
ANISOU 78 CB BGLN A 34 2109 1915 2040 -98 -7 26 C
ATOM 79 CG AGLN A 34 38.867 67.266 45.598 0.50 19.14 C
ANISOU 79 CG AGLN A 34 2516 2308 2447 -82 -11 20 C
ATOM 80 CG BGLN A 34 39.704 68.064 45.876 0.50 17.46 C
ANISOU 80 CG BGLN A 34 2314 2084 2238 -96 -9 19 C
ATOM 81 CD AGLN A 34 39.672 67.937 46.722 0.50 22.21 C
ANISOU 81 CD AGLN A 34 2916 2682 2842 -94 -11 12 C
ATOM 82 CD BGLN A 34 39.466 67.080 47.026 0.50 19.65 C
ANISOU 82 CD BGLN A 34 2581 2368 2519 -88 -14 6 C
ATOM 83 OE1AGLN A 34 40.771 68.437 46.503 0.50 23.77 O
ANISOU 83 OE1AGLN A 34 3114 2876 3039 -113 -9 13 O
ATOM 84 OE1BGLN A 34 38.642 67.330 47.945 0.50 23.37 O
ANISOU 84 OE1BGLN A 34 3061 2827 2993 -76 -15 3 O
ATOM 85 NE2AGLN A 34 39.095 67.964 47.947 0.50 24.94 N
ANISOU 85 NE2AGLN A 34 3268 3017 3192 -84 -14 4 N
ATOM 86 NE2BGLN A 34 40.160 65.978 46.990 0.50 19.30 N
ANISOU 86 NE2BGLN A 34 2519 2342 2474 -94 -15 -2 N
ATOM 87 N PRO A 35 41.680 67.953 41.643 1.00 12.67 N
ANISOU 87 N PRO A 35 1686 1519 1608 -129 5 47 N
ATOM 88 CA PRO A 35 42.048 67.424 40.360 1.00 12.33 C
ANISOU 88 CA PRO A 35 1632 1498 1556 -132 9 52 C
ATOM 89 C PRO A 35 42.004 65.920 40.358 1.00 13.08 C
ANISOU 89 C PRO A 35 1708 1613 1648 -125 6 39 C
ATOM 90 O PRO A 35 42.514 65.267 41.316 1.00 14.24 O
ANISOU 90 O PRO A 35 1846 1762 1802 -127 4 26 O
ATOM 91 CB PRO A 35 43.500 67.924 40.145 1.00 12.82 C
ANISOU 91 CB PRO A 35 1692 1561 1618 -155 15 54 C
ATOM 92 CG PRO A 35 43.883 68.672 41.339 1.00 13.91 C
ANISOU 92 CG PRO A 35 1840 1679 1767 -164 13 49 C
ATOM 93 CD PRO A 35 42.781 68.654 42.339 1.00 12.88 C
ANISOU 93 CD PRO A 35 1718 1535 1642 -148 7 43 C
ATOM 94 N PHE A 36 41.372 65.337 39.371 1.00 12.34 N
ANISOU 94 N PHE A 36 1610 1534 1545 -116 6 43 N
ATOM 95 CA PHE A 36 41.388 63.879 39.163 1.00 13.12 C
ANISOU 95 CA PHE A 36 1692 1652 1641 -110 5 30 C
ATOM 96 C PHE A 36 42.141 63.650 37.872 1.00 13.17 C
ANISOU 96 C PHE A 36 1691 1676 1636 -119 11 34 C
ATOM 97 O PHE A 36 41.534 63.624 36.794 1.00 12.76 O
ANISOU 97 O PHE A 36 1641 1633 1573 -113 12 42 O
ATOM 98 CB PHE A 36 39.958 63.283 39.067 1.00 13.62 C
ANISOU 98 CB PHE A 36 1754 1718 1702 -93 -2 29 C
ATOM 99 CG PHE A 36 39.384 62.836 40.365 1.00 12.56 C
ANISOU 99 CG PHE A 36 1619 1576 1579 -83 -7 20 C
ATOM 100 CD1 PHE A 36 39.069 63.733 41.339 1.00 12.92 C
ANISOU 100 CD1 PHE A 36 1677 1602 1632 -81 -9 23 C
ATOM 101 CD2 PHE A 36 39.029 61.490 40.558 1.00 11.73 C
ANISOU 101 CD2 PHE A 36 1501 1481 1474 -76 -11 8 C
ATOM 102 CE1 PHE A 36 38.505 63.319 42.509 1.00 13.00 C
ANISOU 102 CE1 PHE A 36 1684 1604 1649 -71 -13 15 C
ATOM 103 CE2 PHE A 36 38.453 61.070 41.726 1.00 12.09 C
ANISOU 103 CE2 PHE A 36 1545 1519 1529 -67 -15 1 C
ATOM 104 CZ PHE A 36 38.185 61.983 42.709 1.00 12.82 C
ANISOU 104 CZ PHE A 36 1648 1593 1628 -64 -17 5 C
ATOM 105 N ASP A 37 43.471 63.511 37.977 1.00 12.92 N
ANISOU 105 N ASP A 37 1650 1650 1607 -132 17 30 N
ATOM 106 CA ASP A 37 44.359 63.355 36.825 1.00 13.76 C
ANISOU 106 CA ASP A 37 1749 1774 1703 -142 25 33 C
ATOM 107 C ASP A 37 44.388 61.922 36.349 1.00 13.66 C
ANISOU 107 C ASP A 37 1723 1782 1686 -134 26 21 C
ATOM 108 O ASP A 37 45.327 61.151 36.594 1.00 14.07 O
ANISOU 108 O ASP A 37 1761 1842 1741 -138 30 11 O
ATOM 109 CB ASP A 37 45.746 63.822 37.214 1.00 15.01 C
ANISOU 109 CB ASP A 37 1903 1932 1869 -159 31 34 C
ATOM 110 CG ASP A 37 46.682 63.915 36.062 1.00 16.42 C
ANISOU 110 CG ASP A 37 2075 2126 2037 -170 41 41 C
ATOM 111 OD1 ASP A 37 46.277 63.812 34.894 1.00 17.55 O
ANISOU 111 OD1 ASP A 37 2221 2281 2167 -165 44 47 O
ATOM 112 OD2 ASP A 37 47.877 64.008 36.332 1.00 18.79 O
ANISOU 112 OD2 ASP A 37 2367 2432 2342 -183 45 39 O
ATOM 113 N VAL A 38 43.362 61.570 35.589 1.00 11.76 N
ANISOU 113 N VAL A 38 1486 1547 1435 -123 23 22 N
ATOM 114 CA VAL A 38 43.179 60.187 35.129 1.00 11.66 C
ANISOU 114 CA VAL A 38 1463 1551 1417 -116 23 9 C
ATOM 115 C VAL A 38 42.981 60.025 33.644 1.00 11.94 C
ANISOU 115 C VAL A 38 1499 1604 1434 -115 27 14 C
ATOM 116 O VAL A 38 42.764 58.904 33.170 1.00 12.37 O
ANISOU 116 O VAL A 38 1546 1670 1482 -109 27 2 O
ATOM 117 CB VAL A 38 41.991 59.503 35.867 1.00 11.72 C
ANISOU 117 CB VAL A 38 1471 1552 1432 -102 14 1 C
ATOM 118 CG1 VAL A 38 42.295 59.342 37.358 1.00 12.17 C
ANISOU 118 CG1 VAL A 38 1524 1595 1505 -102 11 -7 C
ATOM 119 CG2 VAL A 38 40.746 60.321 35.657 1.00 11.68 C
ANISOU 119 CG2 VAL A 38 1478 1538 1422 -96 7 13 C
ATOM 120 N GLY A 39 43.134 61.120 32.894 1.00 13.40 N
ANISOU 120 N GLY A 39 1692 1789 1611 -122 31 30 N
ATOM 121 CA GLY A 39 43.075 61.075 31.465 1.00 13.93 C
ANISOU 121 CA GLY A 39 1760 1873 1658 -123 36 36 C
ATOM 122 C GLY A 39 44.384 60.598 30.921 1.00 15.30 C
ANISOU 122 C GLY A 39 1924 2064 1827 -131 47 30 C
ATOM 123 O GLY A 39 45.410 60.672 31.596 1.00 16.48 O
ANISOU 123 O GLY A 39 2066 2208 1987 -139 52 27 O
ATOM 124 N PRO A 40 44.389 60.174 29.646 1.00 15.58 N
ANISOU 124 N PRO A 40 1958 2119 1844 -130 52 29 N
ATOM 125 CA PRO A 40 43.273 60.254 28.720 1.00 15.74 C
ANISOU 125 CA PRO A 40 1985 2147 1847 -124 46 36 C
ATOM 126 C PRO A 40 42.328 59.048 28.768 1.00 14.57 C
ANISOU 126 C PRO A 40 1834 2003 1698 -113 38 19 C
ATOM 127 O PRO A 40 41.253 59.086 28.160 1.00 15.28 O
ANISOU 127 O PRO A 40 1930 2100 1777 -107 30 24 O
ATOM 128 CB PRO A 40 43.966 60.312 27.350 1.00 17.02 C
ANISOU 128 CB PRO A 40 2147 2330 1990 -130 57 41 C
ATOM 129 CG PRO A 40 45.181 59.571 27.531 1.00 17.03 C
ANISOU 129 CG PRO A 40 2136 2340 1996 -134 67 28 C
ATOM 130 CD PRO A 40 45.652 59.849 28.947 1.00 17.95 C
ANISOU 130 CD PRO A 40 2248 2436 2135 -138 65 26 C
ATOM 131 N ARG A 41 42.656 58.004 29.539 1.00 13.53 N
ANISOU 131 N ARG A 41 1694 1868 1578 -110 38 1 N
ATOM 132 CA ARG A 41 41.812 56.831 29.503 1.00 13.63 C
ANISOU 132 CA ARG A 41 1703 1885 1589 -101 31 -14 C
ATOM 133 C ARG A 41 40.450 57.109 30.115 1.00 12.85 C
ANISOU 133 C ARG A 41 1611 1775 1498 -94 18 -9 C
ATOM 134 O ARG A 41 39.420 56.600 29.667 1.00 13.62 O
ANISOU 134 O ARG A 41 1710 1879 1588 -88 10 -13 O
ATOM 135 CB ARG A 41 42.450 55.626 30.206 1.00 13.38 C
ANISOU 135 CB ARG A 41 1662 1852 1571 -98 34 -33 C
ATOM 136 CG ARG A 41 41.553 54.439 30.188 1.00 13.18 C
ANISOU 136 CG ARG A 41 1636 1828 1545 -91 27 -49 C
ATOM 137 CD ARG A 41 42.207 53.212 30.658 1.00 13.27 C
ANISOU 137 CD ARG A 41 1638 1837 1565 -88 32 -67 C
ATOM 138 NE ARG A 41 41.223 52.125 30.754 1.00 13.06 N
ANISOU 138 NE ARG A 41 1612 1809 1541 -81 24 -81 N
ATOM 139 CZ ARG A 41 41.508 50.875 31.052 1.00 14.51 C
ANISOU 139 CZ ARG A 41 1791 1990 1731 -77 28 -98 C
ATOM 140 NH1 ARG A 41 42.776 50.464 31.214 1.00 16.54 N
ANISOU 140 NH1 ARG A 41 2042 2250 1994 -77 39 -104 N
ATOM 141 NH2 ARG A 41 40.526 50.007 31.158 1.00 15.02 N
ANISOU 141 NH2 ARG A 41 1857 2051 1798 -74 20 -108 N
ATOM 142 N TYR A 42 40.447 57.917 31.174 1.00 11.79 N
ANISOU 142 N TYR A 42 1480 1622 1379 -94 15 -1 N
ATOM 143 CA TYR A 42 39.226 58.111 31.925 1.00 11.04 C
ANISOU 143 CA TYR A 42 1388 1514 1293 -86 4 3 C
ATOM 144 C TYR A 42 38.860 59.577 31.885 1.00 11.53 C
ANISOU 144 C TYR A 42 1461 1567 1354 -86 3 23 C
ATOM 145 O TYR A 42 39.695 60.433 32.247 1.00 12.21 O
ANISOU 145 O TYR A 42 1551 1643 1446 -93 9 31 O
ATOM 146 CB TYR A 42 39.387 57.668 33.362 1.00 10.79 C
ANISOU 146 CB TYR A 42 1352 1468 1281 -83 2 -7 C
ATOM 147 CG TYR A 42 39.767 56.191 33.544 1.00 10.34 C
ANISOU 147 CG TYR A 42 1285 1417 1228 -82 4 -27 C
ATOM 148 CD1 TYR A 42 38.814 55.203 33.470 1.00 10.46 C
ANISOU 148 CD1 TYR A 42 1297 1435 1241 -75 -2 -37 C
ATOM 149 CD2 TYR A 42 41.073 55.799 33.731 1.00 10.31 C
ANISOU 149 CD2 TYR A 42 1274 1416 1229 -87 13 -35 C
ATOM 150 CE1 TYR A 42 39.152 53.863 33.647 1.00 10.52 C
ANISOU 150 CE1 TYR A 42 1297 1446 1254 -74 0 -55 C
ATOM 151 CE2 TYR A 42 41.422 54.488 33.886 1.00 10.31 C
ANISOU 151 CE2 TYR A 42 1265 1419 1233 -83 16 -51 C
ATOM 152 CZ TYR A 42 40.454 53.485 33.858 1.00 10.04 C
ANISOU 152 CZ TYR A 42 1231 1386 1199 -77 9 -62 C
ATOM 153 OH TYR A 42 40.805 52.184 34.082 1.00 10.68 O
ANISOU 153 OH TYR A 42 1305 1468 1285 -73 12 -78 O
ATOM 154 N THR A 43 37.636 59.901 31.461 1.00 12.10 N
ANISOU 154 N THR A 43 1538 1642 1418 -78 -5 33 N
ATOM 155 CA THR A 43 37.190 61.316 31.363 1.00 12.76 C
ANISOU 155 CA THR A 43 1632 1715 1500 -76 -6 54 C
ATOM 156 C THR A 43 35.742 61.463 31.812 1.00 12.91 C
ANISOU 156 C THR A 43 1654 1728 1523 -63 -17 59 C
ATOM 157 O THR A 43 35.095 60.469 32.156 1.00 12.53 O
ANISOU 157 O THR A 43 1597 1684 1479 -58 -24 47 O
ATOM 158 CB THR A 43 37.298 61.880 29.922 1.00 13.45 C
ANISOU 158 CB THR A 43 1725 1818 1567 -80 -3 69 C
ATOM 159 OG1 THR A 43 36.318 61.223 29.081 1.00 15.14 O
ANISOU 159 OG1 THR A 43 1936 2051 1767 -73 -11 66 O
ATOM 160 CG2 THR A 43 38.687 61.731 29.352 1.00 13.31 C
ANISOU 160 CG2 THR A 43 1705 1810 1543 -92 9 65 C
ATOM 161 N GLN A 44 35.178 62.641 31.740 1.00 14.41 N
ANISOU 161 N GLN A 44 1854 1909 1713 -58 -19 78 N
ATOM 162 CA GLN A 44 33.785 62.884 32.106 1.00 14.96 C
ANISOU 162 CA GLN A 44 1924 1973 1786 -44 -28 86 C
ATOM 163 C GLN A 44 33.512 62.448 33.542 1.00 14.02 C
ANISOU 163 C GLN A 44 1801 1840 1685 -39 -30 74 C
ATOM 164 O GLN A 44 32.584 61.703 33.868 1.00 13.85 O
ANISOU 164 O GLN A 44 1772 1824 1667 -31 -38 67 O
ATOM 165 CB GLN A 44 32.820 62.256 31.075 1.00 17.59 C
ANISOU 165 CB GLN A 44 2250 2330 2103 -39 -36 87 C
ATOM 166 CG GLN A 44 32.661 63.138 29.876 1.00 21.17 C
ANISOU 166 CG GLN A 44 2712 2794 2540 -38 -36 107 C
ATOM 167 CD GLN A 44 33.839 63.074 28.962 1.00 25.35 C
ANISOU 167 CD GLN A 44 3243 3334 3057 -51 -27 105 C
ATOM 168 OE1 GLN A 44 34.117 62.013 28.403 1.00 29.50 O
ANISOU 168 OE1 GLN A 44 3760 3878 3573 -56 -27 90 O
ATOM 169 NE2 GLN A 44 34.564 64.210 28.784 1.00 28.85 N
ANISOU 169 NE2 GLN A 44 3696 3767 3499 -56 -18 121 N
ATOM 170 N LEU A 45 34.317 63.025 34.420 1.00 13.86 N
ANISOU 170 N LEU A 45 1787 1801 1677 -43 -24 73 N
ATOM 171 CA LEU A 45 34.274 62.753 35.841 1.00 13.98 C
ANISOU 171 CA LEU A 45 1802 1802 1710 -40 -25 62 C
ATOM 172 C LEU A 45 33.051 63.403 36.476 1.00 14.89 C
ANISOU 172 C LEU A 45 1922 1905 1831 -25 -30 72 C
ATOM 173 O LEU A 45 32.735 64.594 36.197 1.00 15.59 O
ANISOU 173 O LEU A 45 2022 1985 1917 -20 -29 89 O
ATOM 174 CB LEU A 45 35.548 63.292 36.533 1.00 15.06 C
ANISOU 174 CB LEU A 45 1943 1923 1855 -51 -18 59 C
ATOM 175 CG LEU A 45 36.875 62.525 36.403 1.00 16.13 C
ANISOU 175 CG LEU A 45 2071 2069 1991 -64 -12 46 C
ATOM 176 CD1 LEU A 45 36.926 61.427 37.421 1.00 16.77 C
ANISOU 176 CD1 LEU A 45 2141 2148 2081 -62 -15 29 C
ATOM 177 CD2 LEU A 45 37.187 61.953 35.019 1.00 16.08 C
ANISOU 177 CD2 LEU A 45 2058 2083 1968 -70 -10 45 C
ATOM 178 N GLN A 46 32.387 62.669 37.336 1.00 14.01 N
ANISOU 178 N GLN A 46 1802 1792 1727 -18 -35 62 N
ATOM 179 CA GLN A 46 31.233 63.144 38.080 1.00 15.08 C
ANISOU 179 CA GLN A 46 1942 1918 1871 -3 -38 70 C
ATOM 180 C GLN A 46 31.364 62.708 39.516 1.00 13.43 C
ANISOU 180 C GLN A 46 1731 1698 1676 -2 -38 57 C
ATOM 181 O GLN A 46 31.637 61.532 39.802 1.00 14.42 O
ANISOU 181 O GLN A 46 1844 1830 1803 -6 -39 42 O
ATOM 182 CB GLN A 46 29.900 62.642 37.460 1.00 17.34 C
ANISOU 182 CB GLN A 46 2217 2221 2149 7 -47 75 C
ATOM 183 CG GLN A 46 29.744 63.059 36.002 1.00 21.17 C
ANISOU 183 CG GLN A 46 2705 2721 2618 6 -49 88 C
ATOM 184 CD GLN A 46 28.634 62.312 35.284 1.00 25.18 C
ANISOU 184 CD GLN A 46 3200 3250 3116 11 -58 89 C
ATOM 185 OE1 GLN A 46 27.798 61.668 35.914 1.00 27.63 O
ANISOU 185 OE1 GLN A 46 3502 3563 3434 18 -63 84 O
ATOM 186 NE2 GLN A 46 28.640 62.379 33.943 1.00 28.11 N
ANISOU 186 NE2 GLN A 46 3572 3639 3471 7 -60 97 N
ATOM 187 N TYR A 47 31.224 63.639 40.435 1.00 12.33 N
ANISOU 187 N TYR A 47 1602 1538 1544 5 -35 62 N
ATOM 188 CA TYR A 47 31.276 63.323 41.861 1.00 11.65 C
ANISOU 188 CA TYR A 47 1515 1441 1470 7 -34 50 C
ATOM 189 C TYR A 47 30.249 62.275 42.363 1.00 11.78 C
ANISOU 189 C TYR A 47 1518 1467 1490 17 -39 45 C
ATOM 190 O TYR A 47 29.074 62.295 41.928 1.00 13.26 O
ANISOU 190 O TYR A 47 1701 1663 1674 28 -44 54 O
ATOM 191 CB TYR A 47 31.029 64.617 42.646 1.00 11.77 C
ANISOU 191 CB TYR A 47 1547 1435 1492 16 -30 58 C
ATOM 192 CG TYR A 47 30.951 64.532 44.132 1.00 12.15 C
ANISOU 192 CG TYR A 47 1596 1470 1549 21 -29 49 C
ATOM 193 CD1 TYR A 47 29.753 64.232 44.773 1.00 12.55 C
ANISOU 193 CD1 TYR A 47 1642 1523 1604 36 -32 50 C
ATOM 194 CD2 TYR A 47 32.058 64.838 44.919 1.00 12.68 C
ANISOU 194 CD2 TYR A 47 1672 1525 1622 10 -26 40 C
ATOM 195 CE1 TYR A 47 29.666 64.248 46.136 1.00 12.50 C
ANISOU 195 CE1 TYR A 47 1638 1505 1605 41 -30 42 C
ATOM 196 CE2 TYR A 47 32.016 64.814 46.283 1.00 13.09 C
ANISOU 196 CE2 TYR A 47 1727 1567 1681 14 -25 31 C
ATOM 197 CZ TYR A 47 30.801 64.535 46.909 1.00 12.66 C
ANISOU 197 CZ TYR A 47 1668 1513 1629 30 -26 33 C
ATOM 198 OH TYR A 47 30.780 64.644 48.269 1.00 15.61 O
ANISOU 198 OH TYR A 47 2046 1875 2008 35 -25 25 O
ATOM 199 N ILE A 48 30.711 61.353 43.214 1.00 12.11 N
ANISOU 199 N ILE A 48 1553 1509 1539 12 -39 30 N
ATOM 200 CA ILE A 48 29.814 60.451 43.893 1.00 12.09 C
ANISOU 200 CA ILE A 48 1540 1512 1543 21 -43 25 C
ATOM 201 C ILE A 48 29.792 60.761 45.370 1.00 11.83 C
ANISOU 201 C ILE A 48 1513 1464 1519 27 -40 22 C
ATOM 202 O ILE A 48 28.720 60.858 45.993 1.00 13.21 O
ANISOU 202 O ILE A 48 1686 1636 1697 40 -41 26 O
ATOM 203 CB ILE A 48 30.189 58.974 43.651 1.00 12.15 C
ANISOU 203 CB ILE A 48 1534 1533 1550 12 -45 12 C
ATOM 204 CG1 ILE A 48 29.934 58.603 42.227 1.00 12.82 C
ANISOU 204 CG1 ILE A 48 1614 1634 1624 8 -49 15 C
ATOM 205 CG2 ILE A 48 29.413 58.096 44.612 1.00 13.09 C
ANISOU 205 CG2 ILE A 48 1644 1652 1676 19 -48 7 C
ATOM 206 CD1 ILE A 48 30.464 57.234 41.830 1.00 12.70 C
ANISOU 206 CD1 ILE A 48 1589 1630 1608 -2 -50 1 C
ATOM 207 N GLY A 49 30.948 60.861 46.044 1.00 11.47 N
ANISOU 207 N GLY A 49 1473 1409 1477 18 -37 13 N
ATOM 208 CA GLY A 49 30.972 61.099 47.453 1.00 11.33 C
ANISOU 208 CA GLY A 49 1461 1379 1466 23 -34 8 C
ATOM 209 C GLY A 49 32.368 61.282 47.973 1.00 11.05 C
ANISOU 209 C GLY A 49 1430 1336 1433 10 -32 0 C
ATOM 210 O GLY A 49 33.317 61.338 47.199 1.00 10.40 O
ANISOU 210 O GLY A 49 1347 1257 1346 -2 -31 -1 O
ATOM 211 N GLU A 50 32.486 61.502 49.249 1.00 11.92 N
ANISOU 211 N GLU A 50 1546 1436 1547 13 -31 -5 N
ATOM 212 CA GLU A 50 33.777 61.766 49.836 1.00 12.59 C
ANISOU 212 CA GLU A 50 1636 1514 1634 0 -30 -13 C
ATOM 213 C GLU A 50 33.781 61.375 51.284 1.00 13.46 C
ANISOU 213 C GLU A 50 1745 1621 1748 4 -30 -21 C
ATOM 214 O GLU A 50 32.736 61.091 51.909 1.00 16.43 O
ANISOU 214 O GLU A 50 2119 1997 2126 18 -30 -20 O
ATOM 215 CB GLU A 50 34.144 63.236 49.680 1.00 13.58 C
ANISOU 215 CB GLU A 50 1778 1624 1757 -5 -27 -8 C
ATOM 216 CG GLU A 50 33.269 64.132 50.493 1.00 14.87 C
ANISOU 216 CG GLU A 50 1956 1771 1921 8 -24 -5 C
ATOM 217 CD GLU A 50 33.391 65.586 50.077 1.00 15.43 C
ANISOU 217 CD GLU A 50 2046 1827 1992 6 -21 3 C
ATOM 218 OE1 GLU A 50 34.325 66.255 50.529 1.00 18.81 O
ANISOU 218 OE1 GLU A 50 2485 2243 2421 -6 -20 -2 O
ATOM 219 OE2 GLU A 50 32.573 66.037 49.241 1.00 16.81 O
ANISOU 219 OE2 GLU A 50 2223 1999 2163 15 -20 15 O
ATOM 220 N GLY A 51 34.971 61.347 51.837 1.00 12.59 N
ANISOU 220 N GLY A 51 1636 1510 1639 -7 -31 -29 N
ATOM 221 CA GLY A 51 35.165 60.938 53.229 1.00 12.89 C
ANISOU 221 CA GLY A 51 1672 1547 1679 -5 -32 -37 C
ATOM 222 C GLY A 51 36.634 61.181 53.597 1.00 13.58 C
ANISOU 222 C GLY A 51 1760 1633 1766 -21 -34 -44 C
ATOM 223 O GLY A 51 37.406 61.783 52.829 1.00 14.04 O
ANISOU 223 O GLY A 51 1822 1689 1822 -34 -33 -43 O
ATOM 224 N ALA A 52 37.035 60.710 54.767 1.00 14.58 N
ANISOU 224 N ALA A 52 1884 1763 1894 -22 -36 -52 N
ATOM 225 CA ALA A 52 38.412 60.907 55.216 1.00 16.17 C
ANISOU 225 CA ALA A 52 2085 1966 2095 -37 -38 -58 C
ATOM 226 C ALA A 52 39.375 60.267 54.186 1.00 14.06 C
ANISOU 226 C ALA A 52 1803 1711 1828 -48 -38 -58 C
ATOM 227 O ALA A 52 40.453 60.797 53.893 1.00 16.12 O
ANISOU 227 O ALA A 52 2065 1972 2088 -62 -39 -59 O
ATOM 228 CB ALA A 52 38.598 60.277 56.618 1.00 17.66 C
ANISOU 228 CB ALA A 52 2268 2159 2283 -33 -42 -65 C
ATOM 229 N TYR A 53 38.963 59.137 53.610 1.00 14.22 N
ANISOU 229 N TYR A 53 1811 1742 1851 -40 -38 -56 N
ATOM 230 CA TYR A 53 39.744 58.430 52.597 1.00 13.07 C
ANISOU 230 CA TYR A 53 1652 1608 1706 -47 -36 -56 C
ATOM 231 C TYR A 53 40.156 59.269 51.373 1.00 12.47 C
ANISOU 231 C TYR A 53 1581 1530 1625 -57 -33 -51 C
ATOM 232 O TYR A 53 41.174 58.948 50.775 1.00 13.29 O
ANISOU 232 O TYR A 53 1676 1644 1730 -67 -32 -53 O
ATOM 233 CB TYR A 53 38.991 57.193 52.091 1.00 12.88 C
ANISOU 233 CB TYR A 53 1617 1591 1683 -37 -35 -56 C
ATOM 234 CG TYR A 53 37.741 57.541 51.324 1.00 13.04 C
ANISOU 234 CG TYR A 53 1644 1608 1701 -29 -34 -49 C
ATOM 235 CD1 TYR A 53 37.775 57.792 49.976 1.00 14.51 C
ANISOU 235 CD1 TYR A 53 1831 1798 1884 -34 -32 -45 C
ATOM 236 CD2 TYR A 53 36.523 57.603 51.963 1.00 13.45 C
ANISOU 236 CD2 TYR A 53 1700 1654 1754 -17 -35 -47 C
ATOM 237 CE1 TYR A 53 36.627 58.163 49.287 1.00 15.02 C
ANISOU 237 CE1 TYR A 53 1901 1860 1945 -26 -32 -38 C
ATOM 238 CE2 TYR A 53 35.356 57.941 51.245 1.00 14.19 C
ANISOU 238 CE2 TYR A 53 1799 1747 1847 -9 -35 -39 C
ATOM 239 CZ TYR A 53 35.452 58.254 49.924 1.00 14.67 C
ANISOU 239 CZ TYR A 53 1861 1811 1903 -14 -34 -35 C
ATOM 240 OH TYR A 53 34.314 58.599 49.163 1.00 18.62 O
ANISOU 240 OH TYR A 53 2363 2311 2400 -7 -34 -27 O
ATOM 241 N GLY A 54 39.403 60.330 51.017 1.00 11.42 N
ANISOU 241 N GLY A 54 1463 1386 1491 -55 -32 -45 N
ATOM 242 CA GLY A 54 39.546 61.001 49.740 1.00 11.86 C
ANISOU 242 CA GLY A 54 1523 1442 1543 -62 -29 -38 C
ATOM 243 C GLY A 54 38.194 61.240 49.109 1.00 11.41 C
ANISOU 243 C GLY A 54 1472 1380 1483 -49 -28 -30 C
ATOM 244 O GLY A 54 37.253 61.591 49.794 1.00 11.48 O
ANISOU 244 O GLY A 54 1489 1380 1493 -39 -29 -28 O
ATOM 245 N MET A 55 38.074 61.014 47.799 1.00 10.77 N
ANISOU 245 N MET A 55 1386 1308 1397 -50 -26 -25 N
ATOM 246 CA MET A 55 36.850 61.333 47.078 1.00 11.12 C
ANISOU 246 CA MET A 55 1436 1351 1438 -40 -26 -15 C
ATOM 247 C MET A 55 36.623 60.249 46.042 1.00 10.88 C
ANISOU 247 C MET A 55 1392 1337 1403 -38 -27 -16 C
ATOM 248 O MET A 55 37.588 59.767 45.404 1.00 9.72 O
ANISOU 248 O MET A 55 1238 1200 1254 -48 -25 -20 O
ATOM 249 CB MET A 55 37.008 62.678 46.418 1.00 12.14 C
ANISOU 249 CB MET A 55 1579 1471 1563 -46 -23 -5 C
ATOM 250 CG MET A 55 35.781 63.200 45.703 1.00 12.66 C
ANISOU 250 CG MET A 55 1651 1534 1625 -34 -24 6 C
ATOM 251 SD MET A 55 36.001 64.940 45.191 1.00 15.35 S
ANISOU 251 SD MET A 55 2012 1858 1962 -39 -19 20 S
ATOM 252 CE MET A 55 35.978 65.740 46.753 1.00 14.85 C
ANISOU 252 CE MET A 55 1963 1773 1907 -37 -19 14 C
ATOM 253 N VAL A 56 35.351 59.908 45.834 1.00 10.11 N
ANISOU 253 N VAL A 56 1293 1243 1305 -26 -30 -13 N
ATOM 254 CA AVAL A 56 34.980 58.952 44.791 0.50 10.26 C
ANISOU 254 CA AVAL A 56 1302 1278 1319 -25 -31 -14 C
ATOM 255 CA BVAL A 56 34.968 58.943 44.780 0.50 10.48 C
ANISOU 255 CA BVAL A 56 1330 1306 1347 -25 -31 -14 C
ATOM 256 C VAL A 56 34.139 59.643 43.721 1.00 10.51 C
ANISOU 256 C VAL A 56 1339 1312 1343 -21 -33 -2 C
ATOM 257 O VAL A 56 33.240 60.426 44.036 1.00 10.49 O
ANISOU 257 O VAL A 56 1344 1301 1341 -11 -34 7 O
ATOM 258 CB AVAL A 56 34.305 57.671 45.372 0.50 9.98 C
ANISOU 258 CB AVAL A 56 1255 1247 1289 -18 -35 -21 C
ATOM 259 CB BVAL A 56 34.189 57.695 45.294 0.50 10.51 C
ANISOU 259 CB BVAL A 56 1323 1315 1356 -17 -35 -21 C
ATOM 260 CG1AVAL A 56 33.106 58.008 46.233 0.50 9.84 C
ANISOU 260 CG1AVAL A 56 1241 1222 1276 -5 -37 -16 C
ATOM 261 CG1BVAL A 56 34.263 56.555 44.282 0.50 10.40 C
ANISOU 261 CG1BVAL A 56 1298 1315 1337 -21 -36 -26 C
ATOM 262 CG2AVAL A 56 33.876 56.708 44.273 0.50 9.85 C
ANISOU 262 CG2AVAL A 56 1230 1245 1267 -18 -37 -24 C
ATOM 263 CG2BVAL A 56 34.712 57.208 46.618 0.50 10.68 C
ANISOU 263 CG2BVAL A 56 1341 1330 1386 -17 -34 -29 C
ATOM 264 N SER A 57 34.424 59.301 42.481 1.00 10.58 N
ANISOU 264 N SER A 57 1343 1334 1343 -27 -32 -1 N
ATOM 265 CA ASER A 57 33.738 59.856 41.315 0.60 10.92 C
ANISOU 265 CA ASER A 57 1390 1383 1376 -24 -34 10 C
ATOM 266 CA BSER A 57 33.812 59.872 41.269 0.40 10.85 C
ANISOU 266 CA BSER A 57 1382 1375 1367 -25 -33 10 C
ATOM 267 C SER A 57 33.354 58.715 40.398 1.00 11.13 C
ANISOU 267 C SER A 57 1406 1427 1395 -25 -37 5 C
ATOM 268 O SER A 57 33.825 57.583 40.583 1.00 11.07 O
ANISOU 268 O SER A 57 1390 1425 1391 -29 -36 -8 O
ATOM 269 CB ASER A 57 34.690 60.769 40.593 0.60 11.22 C
ANISOU 269 CB ASER A 57 1436 1419 1407 -34 -28 17 C
ATOM 270 CB BSER A 57 34.865 60.658 40.474 0.40 10.99 C
ANISOU 270 CB BSER A 57 1406 1392 1377 -36 -28 16 C
ATOM 271 OG ASER A 57 34.951 61.910 41.404 0.60 11.60 O
ANISOU 271 OG ASER A 57 1497 1449 1462 -34 -26 23 O
ATOM 272 OG BSER A 57 35.849 59.809 39.870 0.40 11.28 O
ANISOU 272 OG BSER A 57 1434 1442 1410 -46 -25 7 O
ATOM 273 N SER A 58 32.476 58.987 39.435 1.00 10.86 N
ANISOU 273 N SER A 58 1373 1403 1352 -20 -41 14 N
ATOM 274 CA SER A 58 32.355 58.118 38.253 1.00 11.21 C
ANISOU 274 CA SER A 58 1409 1466 1385 -25 -43 10 C
ATOM 275 C SER A 58 33.079 58.763 37.089 1.00 11.05 C
ANISOU 275 C SER A 58 1394 1451 1351 -32 -39 17 C
ATOM 276 O SER A 58 33.339 59.970 37.087 1.00 11.03 O
ANISOU 276 O SER A 58 1403 1441 1349 -32 -36 29 O
ATOM 277 CB SER A 58 30.887 57.844 37.924 1.00 11.91 C
ANISOU 277 CB SER A 58 1493 1564 1469 -16 -52 15 C
ATOM 278 OG SER A 58 30.198 59.065 37.694 1.00 13.16 O
ANISOU 278 OG SER A 58 1658 1719 1624 -8 -54 32 O
ATOM 279 N ALA A 59 33.482 57.940 36.132 1.00 10.99 N
ANISOU 279 N ALA A 59 1381 1459 1333 -39 -38 8 N
ATOM 280 CA ALA A 59 34.189 58.325 34.938 1.00 11.34 C
ANISOU 280 CA ALA A 59 1430 1515 1365 -47 -34 13 C
ATOM 281 C ALA A 59 33.827 57.413 33.804 1.00 11.56 C
ANISOU 281 C ALA A 59 1451 1562 1378 -49 -37 6 C
ATOM 282 O ALA A 59 33.447 56.299 34.010 1.00 12.55 O
ANISOU 282 O ALA A 59 1570 1692 1507 -48 -41 -7 O
ATOM 283 CB ALA A 59 35.691 58.258 35.149 1.00 11.15 C
ANISOU 283 CB ALA A 59 1405 1486 1344 -56 -24 6 C
ATOM 284 N TYR A 60 34.037 57.899 32.590 1.00 12.08 N
ANISOU 284 N TYR A 60 1521 1640 1427 -53 -35 15 N
ATOM 285 CA TYR A 60 33.933 57.080 31.389 1.00 12.05 C
ANISOU 285 CA TYR A 60 1514 1657 1406 -57 -37 7 C
ATOM 286 C TYR A 60 35.303 56.514 31.046 1.00 12.69 C
ANISOU 286 C TYR A 60 1593 1743 1485 -65 -26 -6 C
ATOM 287 O TYR A 60 36.281 57.241 30.950 1.00 11.89 O
ANISOU 287 O TYR A 60 1496 1639 1382 -70 -18 2 O
ATOM 288 CB TYR A 60 33.421 57.909 30.227 1.00 12.84 C
ANISOU 288 CB TYR A 60 1619 1770 1488 -55 -40 24 C
ATOM 289 CG TYR A 60 33.157 57.086 28.999 1.00 14.39 C
ANISOU 289 CG TYR A 60 1812 1990 1665 -59 -44 15 C
ATOM 290 CD1 TYR A 60 32.017 56.287 28.893 1.00 15.61 C
ANISOU 290 CD1 TYR A 60 1961 2154 1818 -57 -55 8 C
ATOM 291 CD2 TYR A 60 34.060 57.091 27.938 1.00 15.26 C
ANISOU 291 CD2 TYR A 60 1925 2113 1759 -67 -36 14 C
ATOM 292 CE1 TYR A 60 31.784 55.553 27.762 1.00 15.38 C
ANISOU 292 CE1 TYR A 60 1929 2145 1769 -62 -59 -1 C
ATOM 293 CE2 TYR A 60 33.830 56.350 26.791 1.00 16.85 C
ANISOU 293 CE2 TYR A 60 2125 2336 1941 -70 -39 5 C
ATOM 294 CZ TYR A 60 32.698 55.588 26.719 1.00 16.41 C
ANISOU 294 CZ TYR A 60 2065 2289 1883 -68 -51 -3 C
ATOM 295 OH TYR A 60 32.469 54.842 25.574 1.00 20.26 O
ANISOU 295 OH TYR A 60 2550 2797 2349 -73 -55 -14 O
ATOM 296 N ASP A 61 35.364 55.211 30.918 1.00 11.98 N
ANISOU 296 N ASP A 61 1498 1661 1394 -67 -27 -24 N
ATOM 297 CA ASP A 61 36.570 54.475 30.510 1.00 12.48 C
ANISOU 297 CA ASP A 61 1559 1731 1454 -73 -17 -38 C
ATOM 298 C ASP A 61 36.556 54.294 28.984 1.00 12.96 C
ANISOU 298 C ASP A 61 1621 1813 1491 -77 -15 -39 C
ATOM 299 O ASP A 61 35.707 53.562 28.441 1.00 12.88 O
ANISOU 299 O ASP A 61 1610 1813 1471 -76 -23 -48 O
ATOM 300 CB ASP A 61 36.550 53.112 31.224 1.00 12.54 C
ANISOU 300 CB ASP A 61 1559 1732 1474 -71 -17 -58 C
ATOM 301 CG ASP A 61 37.701 52.220 30.854 1.00 13.53 C
ANISOU 301 CG ASP A 61 1681 1863 1596 -74 -7 -73 C
ATOM 302 OD1 ASP A 61 38.530 52.575 29.967 1.00 13.19 O
ANISOU 302 OD1 ASP A 61 1640 1831 1540 -79 2 -70 O
ATOM 303 OD2 ASP A 61 37.838 51.154 31.517 1.00 14.38 O
ANISOU 303 OD2 ASP A 61 1784 1963 1717 -72 -6 -88 O
ATOM 304 N HIS A 62 37.435 55.005 28.298 1.00 14.00 N
ANISOU 304 N HIS A 62 1756 1952 1612 -82 -6 -30 N
ATOM 305 CA HIS A 62 37.503 54.951 26.838 1.00 15.32 C
ANISOU 305 CA HIS A 62 1926 2140 1753 -85 -4 -30 C
ATOM 306 C HIS A 62 38.018 53.630 26.296 1.00 15.65 C
ANISOU 306 C HIS A 62 1965 2193 1788 -88 2 -52 C
ATOM 307 O HIS A 62 37.873 53.368 25.112 1.00 17.34 O
ANISOU 307 O HIS A 62 2182 2426 1980 -90 2 -56 O
ATOM 308 CB HIS A 62 38.356 56.087 26.307 1.00 15.74 C
ANISOU 308 CB HIS A 62 1984 2197 1798 -90 6 -13 C
ATOM 309 CG HIS A 62 37.719 57.404 26.488 1.00 17.01 C
ANISOU 309 CG HIS A 62 2152 2350 1961 -88 0 10 C
ATOM 310 ND1 HIS A 62 36.764 57.894 25.608 1.00 18.50 N
ANISOU 310 ND1 HIS A 62 2345 2551 2133 -85 -8 24 N
ATOM 311 CD2 HIS A 62 37.844 58.331 27.466 1.00 16.62 C
ANISOU 311 CD2 HIS A 62 2105 2281 1929 -87 1 22 C
ATOM 312 CE1 HIS A 62 36.351 59.072 26.032 1.00 19.42 C
ANISOU 312 CE1 HIS A 62 2467 2655 2257 -81 -11 43 C
ATOM 313 NE2 HIS A 62 36.993 59.362 27.158 1.00 17.37 N
ANISOU 313 NE2 HIS A 62 2207 2375 2018 -82 -6 42 N
ATOM 314 N VAL A 63 38.641 52.794 27.116 1.00 14.56 N
ANISOU 314 N VAL A 63 1821 2044 1666 -86 7 -67 N
ATOM 315 CA VAL A 63 39.055 51.482 26.659 1.00 15.51 C
ANISOU 315 CA VAL A 63 1939 2172 1781 -86 13 -89 C
ATOM 316 C VAL A 63 37.880 50.547 26.717 1.00 15.51 C
ANISOU 316 C VAL A 63 1940 2171 1782 -85 1 -102 C
ATOM 317 O VAL A 63 37.454 49.956 25.691 1.00 15.72 O
ANISOU 317 O VAL A 63 1969 2212 1790 -88 -2 -113 O
ATOM 318 CB VAL A 63 40.242 50.954 27.502 1.00 15.88 C
ANISOU 318 CB VAL A 63 1979 2207 1845 -85 24 -99 C
ATOM 319 CG1 VAL A 63 40.520 49.507 27.167 1.00 15.97 C
ANISOU 319 CG1 VAL A 63 1990 2223 1855 -82 29 -122 C
ATOM 320 CG2 VAL A 63 41.479 51.826 27.270 1.00 16.27 C
ANISOU 320 CG2 VAL A 63 2028 2263 1892 -88 37 -87 C
ATOM 321 N ARG A 64 37.283 50.390 27.888 1.00 14.91 N
ANISOU 321 N ARG A 64 1861 2078 1726 -81 -6 -102 N
ATOM 322 CA ARG A 64 36.177 49.451 28.036 1.00 15.31 C
ANISOU 322 CA ARG A 64 1911 2127 1781 -81 -17 -114 C
ATOM 323 C ARG A 64 34.812 49.983 27.581 1.00 14.25 C
ANISOU 323 C ARG A 64 1777 2002 1634 -82 -31 -103 C
ATOM 324 O ARG A 64 33.876 49.223 27.468 1.00 14.85 O
ANISOU 324 O ARG A 64 1852 2081 1709 -84 -41 -112 O
ATOM 325 CB ARG A 64 36.084 48.995 29.484 1.00 16.79 C
ANISOU 325 CB ARG A 64 2092 2293 1993 -77 -19 -118 C
ATOM 326 CG ARG A 64 37.278 48.157 29.911 1.00 18.23 C
ANISOU 326 CG ARG A 64 2272 2468 2186 -75 -7 -132 C
ATOM 327 CD ARG A 64 37.237 47.788 31.397 1.00 21.28 C
ANISOU 327 CD ARG A 64 2654 2835 2597 -70 -8 -133 C
ATOM 328 NE ARG A 64 35.922 47.268 31.770 1.00 23.40 N
ANISOU 328 NE ARG A 64 2921 3098 2872 -70 -20 -136 N
ATOM 329 CZ ARG A 64 35.270 47.556 32.906 1.00 22.04 C
ANISOU 329 CZ ARG A 64 2746 2913 2715 -66 -27 -127 C
ATOM 330 NH1 ARG A 64 35.808 48.340 33.845 1.00 21.23 N
ANISOU 330 NH1 ARG A 64 2642 2801 2624 -62 -23 -116 N
ATOM 331 NH2 ARG A 64 34.088 47.006 33.105 1.00 27.82 N
ANISOU 331 NH2 ARG A 64 3477 3644 3451 -67 -37 -131 N
ATOM 332 N LYS A 65 34.706 51.289 27.336 1.00 15.10 N
ANISOU 332 N LYS A 65 1887 2114 1735 -81 -33 -81 N
ATOM 333 CA LYS A 65 33.504 51.955 26.837 1.00 15.32 C
ANISOU 333 CA LYS A 65 1916 2153 1752 -80 -45 -67 C
ATOM 334 C LYS A 65 32.363 51.808 27.812 1.00 15.36 C
ANISOU 334 C LYS A 65 1916 2147 1773 -75 -56 -64 C
ATOM 335 O LYS A 65 31.258 51.371 27.462 1.00 16.01 O
ANISOU 335 O LYS A 65 1995 2239 1848 -77 -68 -68 O
ATOM 336 CB LYS A 65 33.097 51.405 25.447 1.00 17.30 C
ANISOU 336 CB LYS A 65 2169 2426 1977 -85 -50 -76 C
ATOM 337 CG LYS A 65 34.189 51.425 24.419 1.00 19.66 C
ANISOU 337 CG LYS A 65 2473 2738 2258 -89 -38 -80 C
ATOM 338 CD LYS A 65 34.752 52.758 24.175 1.00 21.17 C
ANISOU 338 CD LYS A 65 2669 2932 2444 -88 -31 -58 C
ATOM 339 CE LYS A 65 35.575 52.693 22.897 1.00 22.51 C
ANISOU 339 CE LYS A 65 2842 3121 2589 -93 -22 -62 C
ATOM 340 NZ LYS A 65 36.397 53.922 22.764 1.00 24.28 N
ANISOU 340 NZ LYS A 65 3070 3344 2811 -93 -12 -41 N
ATOM 341 N THR A 66 32.639 52.133 29.059 1.00 14.13 N
ANISOU 341 N THR A 66 1759 1972 1638 -71 -53 -60 N
ATOM 342 CA THR A 66 31.652 52.034 30.104 1.00 14.61 C
ANISOU 342 CA THR A 66 1815 2022 1716 -65 -61 -57 C
ATOM 343 C THR A 66 32.038 52.999 31.211 1.00 13.26 C
ANISOU 343 C THR A 66 1645 1832 1560 -59 -56 -44 C
ATOM 344 O THR A 66 33.191 53.393 31.322 1.00 13.07 O
ANISOU 344 O THR A 66 1625 1803 1539 -61 -46 -43 O
ATOM 345 CB THR A 66 31.515 50.594 30.663 1.00 16.46 C
ANISOU 345 CB THR A 66 2044 2249 1962 -68 -62 -77 C
ATOM 346 OG1 THR A 66 30.309 50.495 31.433 1.00 19.47 O
ANISOU 346 OG1 THR A 66 2419 2625 2354 -64 -72 -72 O
ATOM 347 CG2 THR A 66 32.678 50.245 31.494 1.00 16.78 C
ANISOU 347 CG2 THR A 66 2084 2274 2017 -67 -51 -85 C
ATOM 348 N ARG A 67 31.094 53.356 32.043 1.00 12.46 N
ANISOU 348 N ARG A 67 1541 1722 1470 -53 -63 -35 N
ATOM 349 CA ARG A 67 31.382 54.176 33.210 1.00 11.57 C
ANISOU 349 CA ARG A 67 1431 1592 1373 -47 -59 -25 C
ATOM 350 C ARG A 67 31.786 53.286 34.380 1.00 10.94 C
ANISOU 350 C ARG A 67 1347 1498 1311 -47 -55 -39 C
ATOM 351 O ARG A 67 31.290 52.161 34.553 1.00 11.12 O
ANISOU 351 O ARG A 67 1365 1523 1339 -48 -59 -51 O
ATOM 352 CB ARG A 67 30.218 55.088 33.572 1.00 12.09 C
ANISOU 352 CB ARG A 67 1498 1655 1442 -37 -66 -8 C
ATOM 353 CG ARG A 67 30.005 56.206 32.532 1.00 13.02 C
ANISOU 353 CG ARG A 67 1621 1783 1543 -35 -68 10 C
ATOM 354 CD ARG A 67 29.025 57.301 32.975 1.00 13.66 C
ANISOU 354 CD ARG A 67 1704 1857 1628 -24 -72 29 C
ATOM 355 NE ARG A 67 29.543 58.151 34.067 1.00 13.01 N
ANISOU 355 NE ARG A 67 1629 1753 1561 -19 -65 35 N
ATOM 356 CZ ARG A 67 30.408 59.171 33.946 1.00 12.38 C
ANISOU 356 CZ ARG A 67 1560 1664 1480 -21 -57 45 C
ATOM 357 NH1 ARG A 67 30.887 59.511 32.775 1.00 13.25 N
ANISOU 357 NH1 ARG A 67 1674 1786 1575 -27 -55 51 N
ATOM 358 NH2 ARG A 67 30.748 59.854 35.022 1.00 12.48 N
ANISOU 358 NH2 ARG A 67 1579 1657 1506 -18 -52 48 N
ATOM 359 N VAL A 68 32.712 53.810 35.158 1.00 10.04 N
ANISOU 359 N VAL A 68 1237 1371 1207 -46 -48 -36 N
ATOM 360 CA VAL A 68 33.353 53.130 36.278 1.00 10.22 C
ANISOU 360 CA VAL A 68 1256 1382 1246 -46 -43 -47 C
ATOM 361 C VAL A 68 33.396 54.087 37.470 1.00 9.78 C
ANISOU 361 C VAL A 68 1204 1310 1202 -40 -42 -37 C
ATOM 362 O VAL A 68 33.145 55.289 37.299 1.00 10.12 O
ANISOU 362 O VAL A 68 1254 1352 1241 -38 -43 -23 O
ATOM 363 CB VAL A 68 34.792 52.695 35.913 1.00 10.72 C
ANISOU 363 CB VAL A 68 1319 1448 1307 -52 -34 -57 C
ATOM 364 CG1 VAL A 68 34.758 51.613 34.828 1.00 10.92 C
ANISOU 364 CG1 VAL A 68 1341 1486 1320 -56 -34 -71 C
ATOM 365 CG2 VAL A 68 35.653 53.905 35.522 1.00 10.71 C
ANISOU 365 CG2 VAL A 68 1324 1447 1299 -56 -27 -46 C
ATOM 366 N ALA A 69 33.722 53.565 38.649 1.00 9.47 N
ANISOU 366 N ALA A 69 1162 1261 1177 -38 -40 -44 N
ATOM 367 CA ALA A 69 34.020 54.399 39.802 1.00 9.43 C
ANISOU 367 CA ALA A 69 1161 1241 1182 -35 -38 -38 C
ATOM 368 C ALA A 69 35.524 54.576 39.889 1.00 9.61 C
ANISOU 368 C ALA A 69 1184 1261 1206 -42 -30 -41 C
ATOM 369 O ALA A 69 36.281 53.647 39.646 1.00 9.54 O
ANISOU 369 O ALA A 69 1169 1257 1197 -46 -26 -52 O
ATOM 370 CB ALA A 69 33.493 53.775 41.096 1.00 9.18 C
ANISOU 370 CB ALA A 69 1124 1200 1164 -29 -41 -42 C
ATOM 371 N ILE A 70 35.949 55.790 40.219 1.00 8.93 N
ANISOU 371 N ILE A 70 1105 1167 1121 -44 -28 -32 N
ATOM 372 CA ILE A 70 37.379 56.064 40.497 1.00 9.40 C
ANISOU 372 CA ILE A 70 1165 1224 1184 -52 -22 -34 C
ATOM 373 C ILE A 70 37.470 56.873 41.766 1.00 9.77 C
ANISOU 373 C ILE A 70 1217 1255 1239 -50 -22 -30 C
ATOM 374 O ILE A 70 36.873 57.916 41.900 1.00 9.63 O
ANISOU 374 O ILE A 70 1209 1229 1221 -47 -24 -20 O
ATOM 375 CB ILE A 70 38.015 56.857 39.368 1.00 9.91 C
ANISOU 375 CB ILE A 70 1234 1295 1237 -60 -17 -27 C
ATOM 376 CG1 ILE A 70 37.786 56.186 38.012 1.00 10.58 C
ANISOU 376 CG1 ILE A 70 1315 1395 1308 -61 -16 -30 C
ATOM 377 CG2 ILE A 70 39.505 57.079 39.681 1.00 9.81 C
ANISOU 377 CG2 ILE A 70 1219 1281 1228 -69 -10 -29 C
ATOM 378 CD1 ILE A 70 38.545 56.858 36.871 1.00 10.95 C
ANISOU 378 CD1 ILE A 70 1366 1452 1343 -69 -10 -23 C
ATOM 379 N LYS A 71 38.257 56.364 42.732 1.00 8.54 N
ANISOU 379 N LYS A 71 1056 1096 1092 -52 -21 -38 N
ATOM 380 CA LYS A 71 38.494 57.085 43.926 1.00 8.57 C
ANISOU 380 CA LYS A 71 1065 1087 1104 -53 -22 -36 C
ATOM 381 C LYS A 71 39.931 57.574 43.998 1.00 8.59 C
ANISOU 381 C LYS A 71 1067 1090 1106 -65 -17 -37 C
ATOM 382 O LYS A 71 40.873 56.823 43.618 1.00 8.87 O
ANISOU 382 O LYS A 71 1092 1136 1142 -69 -13 -43 O
ATOM 383 CB LYS A 71 38.134 56.240 45.183 1.00 8.48 C
ANISOU 383 CB LYS A 71 1048 1071 1102 -45 -25 -43 C
ATOM 384 CG LYS A 71 38.893 54.927 45.347 1.00 8.42 C
ANISOU 384 CG LYS A 71 1029 1072 1099 -46 -23 -54 C
ATOM 385 CD LYS A 71 38.260 54.082 46.445 1.00 8.29 C
ANISOU 385 CD LYS A 71 1008 1051 1090 -37 -27 -58 C
ATOM 386 CE LYS A 71 38.994 52.776 46.648 1.00 8.23 C
ANISOU 386 CE LYS A 71 989 1049 1088 -36 -24 -67 C
ATOM 387 NZ LYS A 71 38.223 51.869 47.552 1.00 8.53 N
ANISOU 387 NZ LYS A 71 1024 1083 1135 -27 -27 -69 N
ATOM 388 N LYS A 72 40.104 58.808 44.500 1.00 8.51 N
ANISOU 388 N LYS A 72 1067 1068 1098 -69 -18 -30 N
ATOM 389 CA LYS A 72 41.409 59.445 44.619 1.00 8.87 C
ANISOU 389 CA LYS A 72 1113 1113 1144 -83 -14 -30 C
ATOM 390 C LYS A 72 41.800 59.375 46.077 1.00 9.20 C
ANISOU 390 C LYS A 72 1153 1148 1194 -84 -18 -36 C
ATOM 391 O LYS A 72 41.147 60.000 46.939 1.00 9.84 O
ANISOU 391 O LYS A 72 1245 1216 1279 -79 -21 -35 O
ATOM 392 CB LYS A 72 41.361 60.909 44.132 1.00 8.78 C
ANISOU 392 CB LYS A 72 1116 1092 1129 -90 -12 -18 C
ATOM 393 CG LYS A 72 42.712 61.580 44.260 1.00 9.18 C
ANISOU 393 CG LYS A 72 1166 1141 1180 -107 -9 -17 C
ATOM 394 CD LYS A 72 42.630 63.056 43.986 1.00 9.44 C
ANISOU 394 CD LYS A 72 1215 1160 1211 -114 -7 -6 C
ATOM 395 CE LYS A 72 44.010 63.679 43.894 1.00 9.90 C
ANISOU 395 CE LYS A 72 1272 1219 1270 -134 -3 -5 C
ATOM 396 NZ LYS A 72 43.863 65.126 43.672 1.00 10.69 N
ANISOU 396 NZ LYS A 72 1390 1302 1369 -141 -1 6 N
ATOM 397 N ILE A 73 42.900 58.726 46.356 1.00 9.39 N
ANISOU 397 N ILE A 73 1164 1181 1221 -90 -16 -42 N
ATOM 398 CA ILE A 73 43.417 58.599 47.697 1.00 9.72 C
ANISOU 398 CA ILE A 73 1203 1220 1269 -91 -20 -48 C
ATOM 399 C ILE A 73 44.799 59.270 47.742 1.00 9.88 C
ANISOU 399 C ILE A 73 1220 1243 1289 -108 -18 -47 C
ATOM 400 O ILE A 73 45.628 59.050 46.853 1.00 9.38 O
ANISOU 400 O ILE A 73 1148 1192 1224 -115 -13 -46 O
ATOM 401 CB ILE A 73 43.627 57.104 48.081 1.00 9.83 C
ANISOU 401 CB ILE A 73 1202 1245 1288 -83 -20 -56 C
ATOM 402 CG1 ILE A 73 42.467 56.184 47.679 1.00 10.43 C
ANISOU 402 CG1 ILE A 73 1277 1321 1364 -69 -21 -57 C
ATOM 403 CG2 ILE A 73 43.970 56.965 49.536 1.00 10.47 C
ANISOU 403 CG2 ILE A 73 1281 1323 1375 -82 -25 -60 C
ATOM 404 CD1 ILE A 73 41.166 56.520 48.305 1.00 10.39 C
ANISOU 404 CD1 ILE A 73 1282 1305 1360 -60 -25 -55 C
ATOM 405 N SER A 74 45.013 60.115 48.743 1.00 10.14 N
ANISOU 405 N SER A 74 1262 1266 1325 -115 -22 -48 N
ATOM 406 CA SER A 74 46.237 60.913 48.857 1.00 11.09 C
ANISOU 406 CA SER A 74 1381 1387 1445 -134 -22 -47 C
ATOM 407 C SER A 74 46.765 60.802 50.289 1.00 10.64 C
ANISOU 407 C SER A 74 1320 1330 1392 -137 -28 -54 C
ATOM 408 O SER A 74 46.592 61.695 51.109 1.00 12.47 O
ANISOU 408 O SER A 74 1565 1549 1624 -142 -32 -55 O
ATOM 409 CB SER A 74 45.932 62.354 48.484 1.00 12.01 C
ANISOU 409 CB SER A 74 1515 1487 1559 -142 -20 -39 C
ATOM 410 OG SER A 74 45.340 62.426 47.190 1.00 12.54 O
ANISOU 410 OG SER A 74 1586 1556 1621 -137 -15 -32 O
ATOM 411 N PRO A 75 47.407 59.652 50.628 1.00 10.07 N
ANISOU 411 N PRO A 75 1230 1274 1323 -133 -29 -58 N
ATOM 412 CA PRO A 75 47.656 59.297 52.005 1.00 10.01 C
ANISOU 412 CA PRO A 75 1218 1268 1318 -131 -36 -64 C
ATOM 413 C PRO A 75 49.064 59.555 52.518 1.00 10.93 C
ANISOU 413 C PRO A 75 1323 1395 1435 -147 -39 -66 C
ATOM 414 O PRO A 75 49.398 59.186 53.636 1.00 10.41 O
ANISOU 414 O PRO A 75 1251 1335 1371 -145 -46 -70 O
ATOM 415 CB PRO A 75 47.432 57.779 51.960 1.00 9.66 C
ANISOU 415 CB PRO A 75 1159 1234 1276 -114 -34 -66 C
ATOM 416 CG PRO A 75 48.061 57.404 50.663 1.00 9.81 C
ANISOU 416 CG PRO A 75 1167 1265 1294 -118 -27 -64 C
ATOM 417 CD PRO A 75 47.670 58.510 49.717 1.00 10.06 C
ANISOU 417 CD PRO A 75 1213 1288 1322 -126 -24 -58 C
ATOM 418 N PHE A 76 49.948 60.091 51.683 1.00 11.36 N
ANISOU 418 N PHE A 76 1373 1456 1489 -162 -35 -62 N
ATOM 419 CA PHE A 76 51.391 59.968 51.907 1.00 13.10 C
ANISOU 419 CA PHE A 76 1575 1692 1710 -176 -37 -62 C
ATOM 420 C PHE A 76 52.000 60.862 53.003 1.00 15.46 C
ANISOU 420 C PHE A 76 1877 1987 2008 -193 -45 -65 C
ATOM 421 O PHE A 76 53.129 60.569 53.464 1.00 16.95 O
ANISOU 421 O PHE A 76 2049 2194 2199 -201 -49 -66 O
ATOM 422 CB PHE A 76 52.128 60.068 50.558 1.00 12.79 C
ANISOU 422 CB PHE A 76 1526 1664 1670 -185 -28 -56 C
ATOM 423 CG PHE A 76 51.738 58.977 49.615 1.00 11.96 C
ANISOU 423 CG PHE A 76 1413 1566 1564 -168 -20 -55 C
ATOM 424 CD1 PHE A 76 51.920 57.647 49.952 1.00 11.55 C
ANISOU 424 CD1 PHE A 76 1346 1526 1515 -153 -20 -59 C
ATOM 425 CD2 PHE A 76 51.156 59.264 48.407 1.00 12.25 C
ANISOU 425 CD2 PHE A 76 1459 1597 1597 -166 -13 -51 C
ATOM 426 CE1 PHE A 76 51.495 56.625 49.100 1.00 11.76 C
ANISOU 426 CE1 PHE A 76 1369 1558 1543 -138 -14 -60 C
ATOM 427 CE2 PHE A 76 50.778 58.236 47.555 1.00 11.28 C
ANISOU 427 CE2 PHE A 76 1330 1482 1472 -152 -7 -52 C
ATOM 428 CZ PHE A 76 50.954 56.926 47.932 1.00 11.03 C
ANISOU 428 CZ PHE A 76 1285 1460 1445 -138 -7 -57 C
ATOM 429 N GLU A 77 51.189 61.762 53.537 1.00 15.30 N
ANISOU 429 N GLU A 77 1880 1948 1987 -194 -49 -68 N
ATOM 430 CA GLU A 77 51.617 62.611 54.656 1.00 17.37 C
ANISOU 430 CA GLU A 77 2149 2204 2247 -210 -58 -73 C
ATOM 431 C GLU A 77 51.592 61.922 55.996 1.00 16.54 C
ANISOU 431 C GLU A 77 2039 2106 2141 -200 -66 -80 C
ATOM 432 O GLU A 77 52.293 62.391 56.925 1.00 16.00 O
ANISOU 432 O GLU A 77 1968 2040 2069 -215 -74 -85 O
ATOM 433 CB GLU A 77 50.809 63.879 54.697 1.00 20.46 C
ANISOU 433 CB GLU A 77 2567 2569 2636 -215 -57 -74 C
ATOM 434 CG GLU A 77 51.003 64.673 53.449 1.00 25.65 C
ANISOU 434 CG GLU A 77 3231 3220 3294 -227 -50 -66 C
ATOM 435 CD GLU A 77 50.344 66.038 53.469 1.00 33.28 C
ANISOU 435 CD GLU A 77 4224 4160 4260 -233 -49 -66 C
ATOM 436 OE1 GLU A 77 49.127 66.161 53.797 1.00 36.83 O
ANISOU 436 OE1 GLU A 77 4691 4595 4709 -217 -48 -67 O
ATOM 437 OE2 GLU A 77 51.065 67.011 53.115 1.00 39.30 O
ANISOU 437 OE2 GLU A 77 4992 4917 5023 -255 -47 -62 O
ATOM 438 N HIS A 78 50.844 60.826 56.157 1.00 15.91 N
ANISOU 438 N HIS A 78 1955 2030 2062 -178 -65 -80 N
ATOM 439 CA AHIS A 78 50.750 60.173 57.438 0.50 15.86 C
ANISOU 439 CA AHIS A 78 1943 2028 2053 -168 -72 -85 C
ATOM 440 CA BHIS A 78 50.800 60.148 57.454 0.50 15.92 C
ANISOU 440 CA BHIS A 78 1950 2037 2061 -169 -72 -85 C
ATOM 441 C HIS A 78 50.834 58.656 57.363 1.00 14.94 C
ANISOU 441 C HIS A 78 1807 1927 1940 -151 -70 -82 C
ATOM 442 O HIS A 78 50.192 58.016 56.504 1.00 13.78 O
ANISOU 442 O HIS A 78 1659 1778 1797 -138 -62 -79 O
ATOM 443 CB AHIS A 78 49.485 60.663 58.127 0.50 16.80 C
ANISOU 443 CB AHIS A 78 2086 2129 2170 -159 -73 -89 C
ATOM 444 CB BHIS A 78 49.620 60.588 58.339 0.50 16.94 C
ANISOU 444 CB BHIS A 78 2101 2149 2187 -160 -75 -90 C
ATOM 445 CG AHIS A 78 49.547 62.120 58.488 0.50 18.30 C
ANISOU 445 CG AHIS A 78 2294 2303 2355 -176 -77 -93 C
ATOM 446 CG BHIS A 78 49.836 60.292 59.807 0.50 18.49 C
ANISOU 446 CG BHIS A 78 2295 2353 2378 -157 -84 -95 C
ATOM 447 ND1AHIS A 78 48.991 63.115 57.703 0.50 20.14 N
ANISOU 447 ND1AHIS A 78 2546 2518 2590 -180 -71 -91 N
ATOM 448 ND1BHIS A 78 49.552 59.064 60.364 0.50 18.85 N
ANISOU 448 ND1BHIS A 78 2330 2409 2425 -139 -85 -93 N
ATOM 449 CD2AHIS A 78 50.173 62.751 59.504 0.50 19.55 C
ANISOU 449 CD2AHIS A 78 2457 2462 2509 -191 -85 -100 C
ATOM 450 CD2BHIS A 78 50.343 61.049 60.817 0.50 19.51 C
ANISOU 450 CD2BHIS A 78 2430 2481 2501 -172 -92 -102 C
ATOM 451 CE1AHIS A 78 49.238 64.290 58.249 0.50 19.80 C
ANISOU 451 CE1AHIS A 78 2518 2462 2543 -197 -75 -96 C
ATOM 452 CE1BHIS A 78 49.876 59.060 61.639 0.50 20.20 C
ANISOU 452 CE1BHIS A 78 2500 2586 2590 -142 -94 -98 C
ATOM 453 NE2AHIS A 78 49.964 64.098 59.333 0.50 19.78 N
ANISOU 453 NE2AHIS A 78 2508 2471 2537 -204 -84 -103 N
ATOM 454 NE2BHIS A 78 50.339 60.266 61.952 0.50 20.62 N
ANISOU 454 NE2BHIS A 78 2563 2633 2638 -161 -99 -104 N
ATOM 455 N GLN A 79 51.572 58.061 58.295 1.00 14.31 N
ANISOU 455 N GLN A 79 1713 1863 1860 -150 -76 -83 N
ATOM 456 CA GLN A 79 51.754 56.664 58.345 1.00 14.50 C
ANISOU 456 CA GLN A 79 1720 1901 1888 -134 -75 -80 C
ATOM 457 C GLN A 79 50.430 55.919 58.459 1.00 13.37 C
ANISOU 457 C GLN A 79 1585 1747 1747 -113 -71 -80 C
ATOM 458 O GLN A 79 50.242 54.868 57.825 1.00 11.77 O
ANISOU 458 O GLN A 79 1374 1549 1550 -100 -65 -77 O
ATOM 459 CB GLN A 79 52.709 56.313 59.455 1.00 17.03 C
ANISOU 459 CB GLN A 79 2025 2239 2206 -137 -84 -80 C
ATOM 460 CG GLN A 79 53.256 54.925 59.407 1.00 19.17 C
ANISOU 460 CG GLN A 79 2274 2527 2483 -123 -81 -75 C
ATOM 461 CD GLN A 79 52.755 54.145 60.504 1.00 24.99 C
ANISOU 461 CD GLN A 79 3012 3265 3219 -107 -86 -75 C
ATOM 462 OE1 GLN A 79 51.563 54.164 60.753 1.00 28.56 O
ANISOU 462 OE1 GLN A 79 3480 3701 3669 -98 -85 -77 O
ATOM 463 NE2 GLN A 79 53.681 53.578 61.331 1.00 31.22 N
ANISOU 463 NE2 GLN A 79 3783 4072 4007 -105 -93 -71 N
ATOM 464 N THR A 80 49.490 56.403 59.274 1.00 12.93 N
ANISOU 464 N THR A 80 1547 1678 1687 -109 -75 -83 N
ATOM 465 CA ATHR A 80 48.250 55.686 59.419 0.50 13.14 C
ANISOU 465 CA ATHR A 80 1581 1697 1716 -90 -71 -82 C
ATOM 466 CA BTHR A 80 48.229 55.741 59.436 0.50 13.30 C
ANISOU 466 CA BTHR A 80 1602 1717 1736 -91 -71 -82 C
ATOM 467 C THR A 80 47.462 55.658 58.108 1.00 12.39 C
ANISOU 467 C THR A 80 1491 1592 1624 -85 -63 -80 C
ATOM 468 O THR A 80 46.854 54.609 57.778 1.00 12.42 O
ANISOU 468 O THR A 80 1490 1597 1633 -71 -58 -78 O
ATOM 469 CB ATHR A 80 47.370 56.190 60.565 0.50 13.71 C
ANISOU 469 CB ATHR A 80 1669 1758 1782 -86 -76 -85 C
ATOM 470 CB BTHR A 80 47.359 56.430 60.490 0.50 14.14 C
ANISOU 470 CB BTHR A 80 1726 1811 1836 -88 -76 -86 C
ATOM 471 OG1ATHR A 80 47.116 57.591 60.411 0.50 14.42 O
ANISOU 471 OG1ATHR A 80 1777 1835 1868 -98 -76 -89 O
ATOM 472 OG1BTHR A 80 48.032 56.400 61.763 0.50 15.61 O
ANISOU 472 OG1BTHR A 80 1907 2007 2016 -92 -84 -88 O
ATOM 473 CG2ATHR A 80 48.025 55.879 61.940 0.50 14.05 C
ANISOU 473 CG2ATHR A 80 1705 1814 1821 -86 -84 -87 C
ATOM 474 CG2BTHR A 80 46.003 55.716 60.589 0.50 14.42 C
ANISOU 474 CG2BTHR A 80 1767 1838 1874 -69 -71 -83 C
ATOM 475 N TYR A 81 47.479 56.750 57.336 1.00 11.06 N
ANISOU 475 N TYR A 81 1332 1415 1454 -97 -60 -80 N
ATOM 476 CA TYR A 81 46.735 56.762 56.107 1.00 10.65 C
ANISOU 476 CA TYR A 81 1287 1357 1405 -93 -53 -77 C
ATOM 477 C TYR A 81 47.348 55.791 55.125 1.00 9.77 C
ANISOU 477 C TYR A 81 1158 1258 1297 -90 -48 -75 C
ATOM 478 O TYR A 81 46.660 55.156 54.343 1.00 8.77 O
ANISOU 478 O TYR A 81 1031 1129 1172 -80 -43 -74 O
ATOM 479 CB TYR A 81 46.743 58.150 55.501 1.00 11.65 C
ANISOU 479 CB TYR A 81 1426 1472 1527 -107 -52 -76 C
ATOM 480 CG TYR A 81 46.331 59.317 56.413 1.00 14.47 C
ANISOU 480 CG TYR A 81 1802 1815 1880 -112 -56 -79 C
ATOM 481 CD1 TYR A 81 45.597 59.138 57.541 1.00 15.52 C
ANISOU 481 CD1 TYR A 81 1942 1943 2012 -101 -60 -82 C
ATOM 482 CD2 TYR A 81 46.657 60.596 56.045 1.00 16.94 C
ANISOU 482 CD2 TYR A 81 2126 2118 2191 -128 -56 -79 C
ATOM 483 CE1 TYR A 81 45.274 60.240 58.369 1.00 17.46 C
ANISOU 483 CE1 TYR A 81 2206 2175 2253 -106 -63 -87 C
ATOM 484 CE2 TYR A 81 46.302 61.691 56.821 1.00 19.39 C
ANISOU 484 CE2 TYR A 81 2456 2412 2498 -133 -59 -83 C
ATOM 485 CZ TYR A 81 45.619 61.482 57.973 1.00 19.46 C
ANISOU 485 CZ TYR A 81 2472 2418 2505 -121 -62 -87 C
ATOM 486 OH TYR A 81 45.284 62.602 58.761 1.00 22.39 O
ANISOU 486 OH TYR A 81 2863 2773 2872 -125 -65 -92 O
ATOM 487 N CYS A 82 48.662 55.684 55.166 1.00 10.00 N
ANISOU 487 N CYS A 82 1173 1301 1327 -100 -49 -75 N
ATOM 488 CA CYS A 82 49.384 54.750 54.310 1.00 10.03 C
ANISOU 488 CA CYS A 82 1159 1317 1333 -96 -43 -73 C
ATOM 489 C CYS A 82 49.084 53.278 54.698 1.00 9.86 C
ANISOU 489 C CYS A 82 1129 1301 1318 -78 -42 -74 C
ATOM 490 O CYS A 82 48.948 52.431 53.808 1.00 9.62 O
ANISOU 490 O CYS A 82 1094 1273 1291 -69 -35 -74 O
ATOM 491 CB CYS A 82 50.875 54.988 54.398 1.00 10.77 C
ANISOU 491 CB CYS A 82 1238 1427 1428 -110 -45 -72 C
ATOM 492 SG CYS A 82 51.436 56.481 53.543 1.00 12.31 S
ANISOU 492 SG CYS A 82 1440 1620 1619 -133 -42 -70 S
ATOM 493 N GLN A 83 48.925 52.988 56.003 1.00 10.25 N
ANISOU 493 N GLN A 83 1179 1350 1368 -72 -49 -74 N
ATOM 494 CA AGLN A 83 48.573 51.636 56.437 0.50 10.25 C
ANISOU 494 CA AGLN A 83 1171 1351 1372 -54 -48 -73 C
ATOM 495 CA BGLN A 83 48.547 51.640 56.473 0.50 10.15 C
ANISOU 495 CA BGLN A 83 1158 1338 1359 -54 -48 -73 C
ATOM 496 C GLN A 83 47.205 51.268 55.831 1.00 9.63 C
ANISOU 496 C GLN A 83 1103 1259 1295 -45 -43 -74 C
ATOM 497 O GLN A 83 47.024 50.158 55.295 1.00 9.01 O
ANISOU 497 O GLN A 83 1019 1182 1222 -34 -37 -75 O
ATOM 498 CB AGLN A 83 48.506 51.543 57.974 0.50 10.70 C
ANISOU 498 CB AGLN A 83 1229 1409 1427 -50 -55 -72 C
ATOM 499 CB BGLN A 83 48.326 51.590 58.006 0.50 10.39 C
ANISOU 499 CB BGLN A 83 1193 1369 1388 -50 -56 -73 C
ATOM 500 CG AGLN A 83 49.862 51.639 58.657 0.50 11.80 C
ANISOU 500 CG AGLN A 83 1355 1565 1565 -58 -61 -71 C
ATOM 501 CG BGLN A 83 49.518 51.856 58.902 0.50 11.29 C
ANISOU 501 CG BGLN A 83 1296 1496 1499 -58 -63 -72 C
ATOM 502 CD AGLN A 83 49.723 51.897 60.137 0.50 13.07 C
ANISOU 502 CD AGLN A 83 1520 1726 1720 -58 -71 -71 C
ATOM 503 CD BGLN A 83 49.210 51.481 60.347 0.50 12.15 C
ANISOU 503 CD BGLN A 83 1406 1606 1605 -49 -70 -70 C
ATOM 504 OE1AGLN A 83 50.701 51.816 60.900 0.50 14.13 O
ANISOU 504 OE1AGLN A 83 1643 1875 1852 -61 -77 -70 O
ATOM 505 OE1BGLN A 83 48.619 50.434 60.617 0.50 13.99 O
ANISOU 505 OE1BGLN A 83 1637 1836 1842 -34 -67 -67 O
ATOM 506 NE2AGLN A 83 48.526 52.256 60.554 0.50 12.53 N
ANISOU 506 NE2AGLN A 83 1468 1643 1648 -53 -71 -73 N
ATOM 507 NE2BGLN A 83 49.581 52.350 61.276 0.50 12.28 N
ANISOU 507 NE2BGLN A 83 1426 1625 1613 -60 -78 -73 N
ATOM 508 N ARG A 84 46.254 52.192 55.885 1.00 9.97 N
ANISOU 508 N ARG A 84 1163 1291 1335 -48 -45 -75 N
ATOM 509 CA ARG A 84 44.866 51.878 55.418 1.00 10.39 C
ANISOU 509 CA ARG A 84 1225 1333 1389 -38 -41 -75 C
ATOM 510 C ARG A 84 44.840 51.693 53.915 1.00 9.05 C
ANISOU 510 C ARG A 84 1054 1165 1220 -40 -35 -75 C
ATOM 511 O ARG A 84 44.110 50.866 53.377 1.00 8.52 O
ANISOU 511 O ARG A 84 986 1095 1155 -32 -32 -76 O
ATOM 512 CB ARG A 84 43.912 52.978 55.834 1.00 11.84 C
ANISOU 512 CB ARG A 84 1425 1506 1569 -40 -44 -74 C
ATOM 513 CG ARG A 84 43.796 53.036 57.361 1.00 14.66 C
ANISOU 513 CG ARG A 84 1785 1861 1924 -36 -50 -74 C
ATOM 514 CD ARG A 84 42.651 53.852 57.805 1.00 19.26 C
ANISOU 514 CD ARG A 84 2384 2432 2503 -33 -51 -74 C
ATOM 515 NE ARG A 84 42.793 54.077 59.243 1.00 22.94 N
ANISOU 515 NE ARG A 84 2853 2899 2965 -32 -56 -75 N
ATOM 516 CZ ARG A 84 42.123 55.007 59.913 1.00 31.11 C
ANISOU 516 CZ ARG A 84 3902 3924 3994 -32 -57 -76 C
ATOM 517 NH1 ARG A 84 41.191 55.738 59.293 1.00 33.17 N
ANISOU 517 NH1 ARG A 84 4175 4173 4254 -30 -54 -75 N
ATOM 518 NH2 ARG A 84 42.392 55.202 61.201 1.00 35.05 N
ANISOU 518 NH2 ARG A 84 4404 4425 4487 -32 -62 -79 N
ATOM 519 N THR A 85 45.667 52.475 53.222 1.00 9.00 N
ANISOU 519 N THR A 85 1046 1164 1210 -52 -33 -75 N
ATOM 520 CA THR A 85 45.755 52.413 51.762 1.00 8.75 C
ANISOU 520 CA THR A 85 1013 1136 1177 -55 -27 -76 C
ATOM 521 C THR A 85 46.374 51.107 51.307 1.00 8.59 C
ANISOU 521 C THR A 85 979 1125 1161 -48 -22 -78 C
ATOM 522 O THR A 85 45.864 50.433 50.392 1.00 8.09 O
ANISOU 522 O THR A 85 916 1060 1097 -43 -17 -81 O
ATOM 523 CB THR A 85 46.525 53.619 51.187 1.00 9.16 C
ANISOU 523 CB THR A 85 1067 1190 1223 -71 -26 -73 C
ATOM 524 OG1 THR A 85 45.905 54.833 51.632 1.00 8.53 O
ANISOU 524 OG1 THR A 85 1002 1098 1140 -77 -30 -71 O
ATOM 525 CG2 THR A 85 46.593 53.596 49.682 1.00 9.06 C
ANISOU 525 CG2 THR A 85 1053 1181 1206 -74 -19 -72 C
ATOM 526 N LEU A 86 47.477 50.742 51.951 1.00 8.80 N
ANISOU 526 N LEU A 86 992 1160 1190 -49 -22 -78 N
ATOM 527 CA LEU A 86 48.122 49.475 51.614 1.00 8.84 C
ANISOU 527 CA LEU A 86 983 1174 1200 -39 -17 -80 C
ATOM 528 C LEU A 86 47.192 48.289 51.904 1.00 8.66 C
ANISOU 528 C LEU A 86 964 1144 1184 -25 -16 -83 C
ATOM 529 O LEU A 86 47.176 47.350 51.136 1.00 9.30 O
ANISOU 529 O LEU A 86 1041 1225 1268 -18 -10 -86 O
ATOM 530 CB LEU A 86 49.460 49.326 52.301 1.00 9.16 C
ANISOU 530 CB LEU A 86 1010 1228 1244 -41 -18 -78 C
ATOM 531 CG LEU A 86 50.243 48.043 52.003 1.00 9.40 C
ANISOU 531 CG LEU A 86 1025 1268 1280 -30 -11 -79 C
ATOM 532 CD1 LEU A 86 50.694 47.969 50.552 1.00 9.51 C
ANISOU 532 CD1 LEU A 86 1035 1288 1291 -32 -1 -82 C
ATOM 533 CD2 LEU A 86 51.443 47.992 52.973 1.00 9.63 C
ANISOU 533 CD2 LEU A 86 1038 1310 1312 -30 -15 -75 C
ATOM 534 N ARG A 87 46.494 48.311 53.021 1.00 8.55 N
ANISOU 534 N ARG A 87 955 1121 1171 -21 -22 -80 N
ATOM 535 CA ARG A 87 45.635 47.198 53.425 1.00 8.28 C
ANISOU 535 CA ARG A 87 922 1079 1143 -8 -22 -81 C
ATOM 536 C ARG A 87 44.509 47.020 52.403 1.00 7.91 C
ANISOU 536 C ARG A 87 885 1025 1096 -7 -19 -84 C
ATOM 537 O ARG A 87 44.216 45.879 51.946 1.00 8.46 O
ANISOU 537 O ARG A 87 953 1092 1171 0 -14 -88 O
ATOM 538 CB ARG A 87 45.081 47.489 54.824 1.00 8.74 C
ANISOU 538 CB ARG A 87 986 1133 1201 -5 -29 -76 C
ATOM 539 CG ARG A 87 44.323 46.316 55.431 1.00 8.25 C
ANISOU 539 CG ARG A 87 923 1064 1146 7 -28 -75 C
ATOM 540 CD ARG A 87 45.077 44.990 55.486 1.00 8.40 C
ANISOU 540 CD ARG A 87 931 1087 1173 17 -24 -75 C
ATOM 541 NE ARG A 87 46.458 45.128 55.933 1.00 8.42 N
ANISOU 541 NE ARG A 87 922 1102 1175 15 -26 -72 N
ATOM 542 CZ ARG A 87 46.860 44.936 57.169 1.00 8.98 C
ANISOU 542 CZ ARG A 87 987 1177 1246 20 -30 -66 C
ATOM 543 NH1 ARG A 87 46.002 44.703 58.141 1.00 9.40 N
ANISOU 543 NH1 ARG A 87 1047 1225 1301 26 -34 -63 N
ATOM 544 NH2 ARG A 87 48.134 45.010 57.453 1.00 9.27 N
ANISOU 544 NH2 ARG A 87 1011 1227 1282 19 -32 -64 N
ATOM 545 N GLU A 88 43.843 48.112 52.034 1.00 7.98 N
ANISOU 545 N GLU A 88 903 1029 1097 -15 -21 -83 N
ATOM 546 CA GLU A 88 42.785 48.117 51.019 1.00 8.14 C
ANISOU 546 CA GLU A 88 932 1046 1116 -15 -20 -85 C
ATOM 547 C GLU A 88 43.296 47.493 49.719 1.00 8.08 C
ANISOU 547 C GLU A 88 920 1044 1107 -16 -13 -91 C
ATOM 548 O GLU A 88 42.661 46.579 49.164 1.00 7.97 O
ANISOU 548 O GLU A 88 906 1027 1095 -11 -10 -95 O
ATOM 549 CB GLU A 88 42.380 49.562 50.685 1.00 8.61 C
ANISOU 549 CB GLU A 88 1002 1103 1168 -24 -22 -82 C
ATOM 550 CG GLU A 88 41.426 49.728 49.499 1.00 9.34 C
ANISOU 550 CG GLU A 88 1100 1193 1254 -25 -21 -82 C
ATOM 551 CD GLU A 88 39.970 49.521 49.839 1.00 9.32 C
ANISOU 551 CD GLU A 88 1104 1183 1254 -18 -25 -80 C
ATOM 552 OE1 GLU A 88 39.647 48.994 50.961 1.00 10.32 O
ANISOU 552 OE1 GLU A 88 1228 1305 1387 -12 -27 -79 O
ATOM 553 OE2 GLU A 88 39.151 49.838 48.986 1.00 10.74 O
ANISOU 553 OE2 GLU A 88 1288 1362 1428 -20 -25 -79 O
ATOM 554 N ILE A 89 44.444 47.941 49.223 1.00 8.26 N
ANISOU 554 N ILE A 89 937 1076 1126 -22 -9 -91 N
ATOM 555 CA ILE A 89 44.971 47.464 47.991 1.00 8.77 C
ANISOU 555 CA ILE A 89 997 1147 1187 -23 -2 -96 C
ATOM 556 C ILE A 89 45.360 45.979 48.084 1.00 8.27 C
ANISOU 556 C ILE A 89 926 1085 1132 -12 3 -102 C
ATOM 557 O ILE A 89 45.040 45.182 47.209 1.00 9.03 O
ANISOU 557 O ILE A 89 1023 1179 1227 -8 8 -109 O
ATOM 558 CB ILE A 89 46.169 48.333 47.534 1.00 9.20 C
ANISOU 558 CB ILE A 89 1047 1214 1237 -33 2 -93 C
ATOM 559 CG1 ILE A 89 45.649 49.728 47.186 1.00 9.32 C
ANISOU 559 CG1 ILE A 89 1072 1225 1243 -43 -2 -88 C
ATOM 560 CG2 ILE A 89 46.892 47.688 46.366 1.00 10.14 C
ANISOU 560 CG2 ILE A 89 1159 1342 1353 -31 11 -99 C
ATOM 561 CD1 ILE A 89 46.752 50.742 46.962 1.00 9.62 C
ANISOU 561 CD1 ILE A 89 1106 1271 1277 -55 0 -84 C
ATOM 562 N GLN A 90 46.140 45.628 49.096 1.00 8.73 N
ANISOU 562 N GLN A 90 975 1146 1197 -7 3 -99 N
ATOM 563 CA GLN A 90 46.672 44.283 49.165 1.00 9.02 C
ANISOU 563 CA GLN A 90 1003 1182 1241 5 9 -102 C
ATOM 564 C GLN A 90 45.544 43.244 49.230 1.00 8.80 C
ANISOU 564 C GLN A 90 983 1142 1220 12 8 -106 C
ATOM 565 O GLN A 90 45.586 42.205 48.597 1.00 9.69 O
ANISOU 565 O GLN A 90 1094 1251 1336 19 15 -113 O
ATOM 566 CB GLN A 90 47.638 44.106 50.313 1.00 9.12 C
ANISOU 566 CB GLN A 90 1004 1200 1260 10 7 -97 C
ATOM 567 CG GLN A 90 48.973 44.788 50.097 1.00 9.74 C
ANISOU 567 CG GLN A 90 1072 1295 1335 3 9 -94 C
ATOM 568 CD GLN A 90 50.054 44.307 50.995 1.00 9.37 C
ANISOU 568 CD GLN A 90 1010 1257 1294 10 8 -89 C
ATOM 569 OE1 GLN A 90 49.972 44.445 52.222 1.00 9.53 O
ANISOU 569 OE1 GLN A 90 1029 1275 1316 11 0 -84 O
ATOM 570 NE2 GLN A 90 51.166 43.881 50.397 1.00 9.69 N
ANISOU 570 NE2 GLN A 90 1038 1308 1336 14 17 -90 N
ATOM 571 N ILE A 91 44.507 43.521 50.016 1.00 8.45 N
ANISOU 571 N ILE A 91 944 1088 1176 12 1 -102 N
ATOM 572 CA ILE A 91 43.357 42.595 50.090 1.00 8.81 C
ANISOU 572 CA ILE A 91 997 1123 1229 17 1 -105 C
ATOM 573 C ILE A 91 42.567 42.580 48.798 1.00 8.63 C
ANISOU 573 C ILE A 91 981 1098 1200 11 2 -112 C
ATOM 574 O ILE A 91 42.311 41.508 48.232 1.00 8.27 O
ANISOU 574 O ILE A 91 937 1046 1157 15 6 -120 O
ATOM 575 CB ILE A 91 42.438 42.934 51.279 1.00 8.72 C
ANISOU 575 CB ILE A 91 989 1105 1219 17 -7 -97 C
ATOM 576 CG1 ILE A 91 43.187 42.654 52.597 1.00 8.46 C
ANISOU 576 CG1 ILE A 91 950 1074 1193 25 -8 -91 C
ATOM 577 CG2 ILE A 91 41.143 42.153 51.207 1.00 9.05 C
ANISOU 577 CG2 ILE A 91 1037 1136 1266 20 -8 -99 C
ATOM 578 CD1 ILE A 91 42.523 43.116 53.851 1.00 8.62 C
ANISOU 578 CD1 ILE A 91 973 1091 1213 25 -15 -83 C
ATOM 579 N LEU A 92 42.153 43.733 48.299 1.00 8.77 N
ANISOU 579 N LEU A 92 1004 1120 1208 2 -2 -110 N
ATOM 580 CA LEU A 92 41.245 43.728 47.179 1.00 9.31 C
ANISOU 580 CA LEU A 92 1080 1188 1270 -2 -2 -115 C
ATOM 581 C LEU A 92 41.861 43.275 45.866 1.00 10.41 C
ANISOU 581 C LEU A 92 1218 1333 1403 -4 6 -124 C
ATOM 582 O LEU A 92 41.181 42.648 45.058 1.00 11.70 O
ANISOU 582 O LEU A 92 1386 1494 1565 -5 6 -132 O
ATOM 583 CB LEU A 92 40.556 45.082 47.000 1.00 9.34 C
ANISOU 583 CB LEU A 92 1089 1194 1265 -10 -8 -109 C
ATOM 584 CG LEU A 92 39.584 45.428 48.126 1.00 9.63 C
ANISOU 584 CG LEU A 92 1129 1223 1306 -7 -14 -101 C
ATOM 585 CD1 LEU A 92 38.931 46.732 47.785 1.00 11.04 C
ANISOU 585 CD1 LEU A 92 1315 1404 1476 -13 -19 -95 C
ATOM 586 CD2 LEU A 92 38.561 44.350 48.361 1.00 9.79 C
ANISOU 586 CD2 LEU A 92 1150 1236 1333 -3 -16 -104 C
ATOM 587 N LEU A 93 43.161 43.474 45.679 1.00 10.14 N
ANISOU 587 N LEU A 93 1177 1308 1367 -3 11 -124 N
ATOM 588 CA LEU A 93 43.779 42.884 44.514 1.00 11.41 C
ANISOU 588 CA LEU A 93 1336 1474 1523 -2 20 -134 C
ATOM 589 C LEU A 93 43.796 41.385 44.514 1.00 12.53 C
ANISOU 589 C LEU A 93 1478 1609 1675 7 26 -143 C
ATOM 590 O LEU A 93 43.935 40.826 43.415 1.00 16.39 O
ANISOU 590 O LEU A 93 1969 2099 2158 7 32 -153 O
ATOM 591 CB LEU A 93 45.245 43.376 44.416 1.00 11.11 C
ANISOU 591 CB LEU A 93 1290 1449 1484 -3 26 -131 C
ATOM 592 CG LEU A 93 45.451 44.835 43.985 1.00 12.30 C
ANISOU 592 CG LEU A 93 1442 1609 1624 -14 24 -124 C
ATOM 593 CD1 LEU A 93 46.917 45.139 43.868 1.00 12.37 C
ANISOU 593 CD1 LEU A 93 1439 1630 1630 -16 31 -121 C
ATOM 594 CD2 LEU A 93 44.783 45.169 42.676 1.00 13.74 C
ANISOU 594 CD2 LEU A 93 1632 1795 1793 -21 25 -127 C
ATOM 595 N AARG A 94 43.660 40.726 45.649 0.50 11.43 N
ANISOU 595 N AARG A 94 1337 1460 1548 14 23 -139 N
ATOM 596 N BARG A 94 43.680 40.741 45.694 0.50 11.92 N
ANISOU 596 N BARG A 94 1398 1521 1610 15 23 -139 N
ATOM 597 CA AARG A 94 43.728 39.276 45.700 0.50 10.94 C
ANISOU 597 CA AARG A 94 1274 1386 1495 24 29 -147 C
ATOM 598 CA BARG A 94 43.824 39.264 45.899 0.50 11.60 C
ANISOU 598 CA BARG A 94 1357 1470 1581 25 29 -146 C
ATOM 599 C AARG A 94 42.319 38.674 45.697 0.50 10.40 C
ANISOU 599 C AARG A 94 1215 1305 1431 21 24 -151 C
ATOM 600 C BARG A 94 42.515 38.590 46.291 0.50 11.55 C
ANISOU 600 C BARG A 94 1358 1449 1581 25 24 -147 C
ATOM 601 O AARG A 94 42.047 37.690 44.990 0.50 10.27 O
ANISOU 601 O AARG A 94 1204 1282 1416 22 29 -162 O
ATOM 602 O BARG A 94 42.471 37.380 46.554 0.50 12.37 O
ANISOU 602 O BARG A 94 1463 1541 1696 32 28 -151 O
ATOM 603 CB AARG A 94 44.589 38.865 46.880 0.50 10.67 C
ANISOU 603 CB AARG A 94 1230 1350 1472 35 31 -140 C
ATOM 604 CB BARG A 94 44.874 38.979 46.948 0.50 11.53 C
ANISOU 604 CB BARG A 94 1338 1463 1581 35 32 -138 C
ATOM 605 CG AARG A 94 46.079 39.264 46.667 0.50 10.79 C
ANISOU 605 CG AARG A 94 1235 1381 1484 37 37 -138 C
ATOM 606 CG BARG A 94 46.253 39.557 46.603 0.50 11.50 C
ANISOU 606 CG BARG A 94 1323 1474 1572 36 37 -137 C
ATOM 607 CD AARG A 94 46.901 39.260 47.936 0.50 10.36 C
ANISOU 607 CD AARG A 94 1169 1329 1437 45 36 -127 C
ATOM 608 CD BARG A 94 47.168 39.443 47.776 0.50 11.14 C
ANISOU 608 CD BARG A 94 1267 1432 1535 44 37 -127 C
ATOM 609 NE AARG A 94 48.352 39.445 47.715 0.50 10.23 N
ANISOU 609 NE AARG A 94 1141 1328 1420 48 42 -126 N
ATOM 610 NE BARG A 94 48.564 39.712 47.430 0.50 11.03 N
ANISOU 610 NE BARG A 94 1240 1433 1517 46 43 -126 N
ATOM 611 CZ AARG A 94 48.967 40.630 47.639 0.50 9.98 C
ANISOU 611 CZ AARG A 94 1102 1310 1380 39 40 -120 C
ATOM 612 CZ BARG A 94 49.031 40.908 47.090 0.50 10.95 C
ANISOU 612 CZ BARG A 94 1226 1436 1497 35 42 -123 C
ATOM 613 NH1AARG A 94 48.286 41.758 47.759 0.50 9.64 N
ANISOU 613 NH1AARG A 94 1066 1267 1329 26 31 -117 N
ATOM 614 NH1BARG A 94 48.221 41.943 47.019 0.50 10.63 N
ANISOU 614 NH1BARG A 94 1194 1394 1449 22 34 -120 N
ATOM 615 NH2AARG A 94 50.266 40.695 47.430 0.50 10.00 N
ANISOU 615 NH2AARG A 94 1091 1326 1381 42 46 -119 N
ATOM 616 NH2BARG A 94 50.310 41.075 46.826 0.50 10.88 N
ANISOU 616 NH2BARG A 94 1204 1442 1486 36 48 -121 N
ATOM 617 N APHE A 95 41.433 39.231 46.514 0.50 9.59 N
ANISOU 617 N APHE A 95 1114 1200 1330 17 16 -142 N
ATOM 618 N BPHE A 95 41.444 39.368 46.271 0.50 10.47 N
ANISOU 618 N BPHE A 95 1226 1313 1439 16 16 -143 N
ATOM 619 CA APHE A 95 40.038 38.745 46.573 0.50 9.53 C
ANISOU 619 CA APHE A 95 1113 1183 1326 13 10 -144 C
ATOM 620 CA BPHE A 95 40.083 38.854 46.475 0.50 10.25 C
ANISOU 620 CA BPHE A 95 1204 1275 1416 13 10 -144 C
ATOM 621 C APHE A 95 39.360 38.846 45.185 0.50 9.75 C
ANISOU 621 C APHE A 95 1147 1214 1342 4 9 -153 C
ATOM 622 C BPHE A 95 39.334 38.881 45.137 0.50 10.14 C
ANISOU 622 C BPHE A 95 1196 1264 1391 4 9 -153 C
ATOM 623 O APHE A 95 39.551 39.816 44.425 0.50 9.44 O
ANISOU 623 O APHE A 95 1108 1187 1291 -1 8 -153 O
ATOM 624 O BPHE A 95 39.480 39.821 44.334 0.50 9.69 O
ANISOU 624 O BPHE A 95 1141 1219 1322 -2 8 -153 O
ATOM 625 CB APHE A 95 39.195 39.597 47.524 0.50 9.26 C
ANISOU 625 CB APHE A 95 1078 1148 1291 11 2 -132 C
ATOM 626 CB BPHE A 95 39.347 39.752 47.473 0.50 10.04 C
ANISOU 626 CB BPHE A 95 1177 1249 1390 10 2 -131 C
ATOM 627 CG APHE A 95 39.343 39.282 48.999 0.50 9.10 C
ANISOU 627 CG APHE A 95 1054 1122 1283 19 1 -122 C
ATOM 628 CG BPHE A 95 39.460 39.306 48.906 0.50 9.88 C
ANISOU 628 CG BPHE A 95 1152 1221 1380 19 1 -123 C
ATOM 629 CD1APHE A 95 40.026 38.187 49.484 0.50 9.00 C
ANISOU 629 CD1APHE A 95 1038 1102 1280 28 7 -123 C
ATOM 630 CD1BPHE A 95 40.247 38.238 49.255 0.50 9.87 C
ANISOU 630 CD1BPHE A 95 1148 1214 1389 28 8 -125 C
ATOM 631 CD2APHE A 95 38.744 40.132 49.909 0.50 8.70 C
ANISOU 631 CD2APHE A 95 1003 1072 1230 17 -6 -112 C
ATOM 632 CD2BPHE A 95 38.798 40.000 49.915 0.50 9.43 C
ANISOU 632 CD2BPHE A 95 1095 1164 1324 18 -5 -113 C
ATOM 633 CE1APHE A 95 40.092 37.953 50.864 0.50 8.90 C
ANISOU 633 CE1APHE A 95 1021 1084 1276 35 5 -113 C
ATOM 634 CE1BPHE A 95 40.320 37.806 50.564 0.50 9.88 C
ANISOU 634 CE1BPHE A 95 1146 1209 1400 35 7 -116 C
ATOM 635 CE2APHE A 95 38.788 39.881 51.258 0.50 8.81 C
ANISOU 635 CE2APHE A 95 1014 1081 1252 24 -7 -104 C
ATOM 636 CE2BPHE A 95 38.890 39.574 51.232 0.50 9.42 C
ANISOU 636 CE2BPHE A 95 1091 1157 1331 25 -6 -105 C
ATOM 637 CZ APHE A 95 39.451 38.803 51.737 0.50 8.77 C
ANISOU 637 CZ APHE A 95 1006 1071 1257 33 -2 -104 C
ATOM 638 CZ BPHE A 95 39.652 38.481 51.551 0.50 9.58 C
ANISOU 638 CZ BPHE A 95 1107 1171 1360 34 0 -106 C
ATOM 639 N ARG A 96 38.507 37.872 44.906 1.00 10.23 N
ANISOU 639 N ARG A 96 1213 1265 1408 1 8 -161 N
ATOM 640 CA ARG A 96 37.613 37.911 43.760 1.00 10.95 C
ANISOU 640 CA ARG A 96 1311 1361 1490 -9 4 -169 C
ATOM 641 C ARG A 96 36.345 37.167 44.144 1.00 9.95 C
ANISOU 641 C ARG A 96 1186 1223 1371 -13 -1 -170 C
ATOM 642 O ARG A 96 36.338 35.930 44.295 1.00 11.01 O
ANISOU 642 O ARG A 96 1322 1344 1516 -11 3 -177 O
ATOM 643 CB ARG A 96 38.265 37.278 42.567 1.00 14.04 C
ANISOU 643 CB ARG A 96 1706 1754 1875 -9 12 -184 C
ATOM 644 CG ARG A 96 37.408 37.339 41.305 1.00 18.58 C
ANISOU 644 CG ARG A 96 2287 2336 2436 -20 7 -194 C
ATOM 645 CD ARG A 96 38.162 36.576 40.226 1.00 23.70 C
ANISOU 645 CD ARG A 96 2940 2984 3078 -18 17 -210 C
ATOM 646 NE ARG A 96 37.499 36.603 38.950 1.00 30.89 N
ANISOU 646 NE ARG A 96 3858 3904 3974 -29 13 -221 N
ATOM 647 CZ ARG A 96 37.993 36.037 37.845 1.00 37.65 C
ANISOU 647 CZ ARG A 96 4721 4763 4821 -29 21 -237 C
ATOM 648 NH1 ARG A 96 39.199 35.430 37.867 1.00 37.33 N
ANISOU 648 NH1 ARG A 96 4679 4717 4785 -18 33 -243 N
ATOM 649 NH2 ARG A 96 37.283 36.074 36.718 1.00 39.15 N
ANISOU 649 NH2 ARG A 96 4917 4963 4996 -40 15 -246 N
ATOM 650 N HIS A 97 35.270 37.927 44.342 1.00 9.42 N
ANISOU 650 N HIS A 97 1117 1161 1301 -19 -10 -161 N
ATOM 651 CA HIS A 97 34.002 37.355 44.770 1.00 9.09 C
ANISOU 651 CA HIS A 97 1076 1112 1267 -24 -16 -159 C
ATOM 652 C HIS A 97 32.882 38.283 44.358 1.00 8.94 C
ANISOU 652 C HIS A 97 1055 1104 1238 -31 -25 -153 C
ATOM 653 O HIS A 97 32.996 39.504 44.433 1.00 8.69 O
ANISOU 653 O HIS A 97 1022 1083 1199 -29 -28 -144 O
ATOM 654 CB HIS A 97 34.031 37.125 46.302 1.00 8.44 C
ANISOU 654 CB HIS A 97 989 1020 1199 -16 -15 -147 C
ATOM 655 CG HIS A 97 32.848 36.417 46.829 1.00 8.35 C
ANISOU 655 CG HIS A 97 977 1000 1197 -20 -18 -144 C
ATOM 656 ND1 HIS A 97 31.635 37.031 47.049 1.00 8.66 N
ANISOU 656 ND1 HIS A 97 1012 1044 1233 -26 -26 -136 N
ATOM 657 CD2 HIS A 97 32.672 35.122 47.141 1.00 8.23 C
ANISOU 657 CD2 HIS A 97 964 970 1195 -21 -15 -149 C
ATOM 658 CE1 HIS A 97 30.762 36.155 47.469 1.00 8.44 C
ANISOU 658 CE1 HIS A 97 983 1008 1215 -30 -28 -134 C
ATOM 659 NE2 HIS A 97 31.371 34.979 47.547 1.00 8.31 N
ANISOU 659 NE2 HIS A 97 971 978 1209 -28 -21 -142 N
ATOM 660 N GLU A 98 31.749 37.700 43.967 1.00 8.99 N
ANISOU 660 N GLU A 98 1062 1110 1245 -41 -31 -158 N
ATOM 661 CA GLU A 98 30.604 38.475 43.531 1.00 9.49 C
ANISOU 661 CA GLU A 98 1123 1185 1299 -47 -40 -152 C
ATOM 662 C GLU A 98 30.095 39.503 44.540 1.00 8.92 C
ANISOU 662 C GLU A 98 1044 1115 1228 -41 -44 -134 C
ATOM 663 O GLU A 98 29.522 40.529 44.158 1.00 9.80 O
ANISOU 663 O GLU A 98 1154 1239 1330 -43 -50 -127 O
ATOM 664 CB GLU A 98 29.429 37.574 43.155 1.00 10.55 C
ANISOU 664 CB GLU A 98 1255 1316 1436 -59 -46 -158 C
ATOM 665 CG GLU A 98 29.638 36.755 41.922 1.00 13.29 C
ANISOU 665 CG GLU A 98 1610 1664 1777 -68 -45 -177 C
ATOM 666 CD GLU A 98 28.480 35.891 41.579 1.00 16.72 C
ANISOU 666 CD GLU A 98 2043 2096 2214 -81 -52 -184 C
ATOM 667 OE1 GLU A 98 27.606 35.576 42.465 1.00 17.86 O
ANISOU 667 OE1 GLU A 98 2181 2234 2370 -83 -55 -175 O
ATOM 668 OE2 GLU A 98 28.522 35.435 40.383 1.00 22.68 O
ANISOU 668 OE2 GLU A 98 2804 2854 2959 -90 -54 -199 O
ATOM 669 N ASN A 99 30.244 39.206 45.833 1.00 8.44 N
ANISOU 669 N ASN A 99 981 1044 1180 -34 -40 -127 N
ATOM 670 CA ASN A 99 29.745 40.096 46.865 1.00 8.10 C
ANISOU 670 CA ASN A 99 934 1005 1140 -28 -43 -112 C
ATOM 671 C ASN A 99 30.824 40.926 47.548 1.00 7.58 C
ANISOU 671 C ASN A 99 870 938 1072 -19 -38 -107 C
ATOM 672 O ASN A 99 30.584 41.456 48.642 1.00 7.32 O
ANISOU 672 O ASN A 99 835 904 1043 -13 -39 -96 O
ATOM 673 CB ASN A 99 28.921 39.309 47.881 1.00 8.03 C
ANISOU 673 CB ASN A 99 920 986 1143 -28 -43 -107 C
ATOM 674 CG ASN A 99 27.770 38.559 47.256 1.00 8.22 C
ANISOU 674 CG ASN A 99 942 1013 1170 -40 -48 -111 C
ATOM 675 OD1 ASN A 99 27.751 37.327 47.285 1.00 8.50 O
ANISOU 675 OD1 ASN A 99 978 1037 1215 -45 -46 -119 O
ATOM 676 ND2 ASN A 99 26.866 39.284 46.595 1.00 8.30 N
ANISOU 676 ND2 ASN A 99 948 1036 1170 -44 -56 -108 N
ATOM 677 N VAL A 100 31.969 41.092 46.884 1.00 7.73 N
ANISOU 677 N VAL A 100 892 959 1085 -19 -34 -114 N
ATOM 678 CA VAL A 100 33.077 41.933 47.367 1.00 7.64 C
ANISOU 678 CA VAL A 100 882 950 1071 -12 -31 -109 C
ATOM 679 C VAL A 100 33.496 42.844 46.200 1.00 7.96 C
ANISOU 679 C VAL A 100 926 1001 1098 -16 -31 -112 C
ATOM 680 O VAL A 100 33.694 42.359 45.087 1.00 8.86 O
ANISOU 680 O VAL A 100 1042 1118 1206 -21 -30 -122 O
ATOM 681 CB VAL A 100 34.245 41.065 47.887 1.00 7.88 C
ANISOU 681 CB VAL A 100 912 973 1110 -7 -24 -114 C
ATOM 682 CG1 VAL A 100 35.367 41.982 48.372 1.00 8.32 C
ANISOU 682 CG1 VAL A 100 966 1033 1162 -2 -22 -109 C
ATOM 683 CG2 VAL A 100 33.824 40.157 49.012 1.00 7.90 C
ANISOU 683 CG2 VAL A 100 911 964 1125 -3 -23 -110 C
ATOM 684 N ILE A 101 33.642 44.142 46.435 1.00 8.00 N
ANISOU 684 N ILE A 101 933 1011 1097 -15 -33 -103 N
ATOM 685 CA ILE A 101 34.049 45.017 45.341 1.00 8.35 C
ANISOU 685 CA ILE A 101 980 1064 1128 -19 -33 -104 C
ATOM 686 C ILE A 101 35.466 44.639 44.918 1.00 8.36 C
ANISOU 686 C ILE A 101 981 1066 1128 -20 -26 -112 C
ATOM 687 O ILE A 101 36.323 44.351 45.746 1.00 8.93 O
ANISOU 687 O ILE A 101 1050 1133 1208 -15 -22 -112 O
ATOM 688 CB ILE A 101 33.942 46.493 45.783 1.00 8.23 C
ANISOU 688 CB ILE A 101 969 1051 1109 -17 -35 -92 C
ATOM 689 CG1 ILE A 101 33.931 47.492 44.595 1.00 8.85 C
ANISOU 689 CG1 ILE A 101 1051 1137 1174 -21 -36 -89 C
ATOM 690 CG2 ILE A 101 34.949 46.847 46.854 1.00 8.29 C
ANISOU 690 CG2 ILE A 101 976 1053 1122 -13 -32 -89 C
ATOM 691 CD1 ILE A 101 32.754 47.334 43.637 1.00 8.83 C
ANISOU 691 CD1 ILE A 101 1048 1142 1164 -24 -42 -89 C
ATOM 692 N GLY A 102 35.700 44.649 43.612 1.00 8.77 N
ANISOU 692 N GLY A 102 1036 1127 1170 -25 -24 -118 N
ATOM 693 CA GLY A 102 37.017 44.386 43.094 1.00 9.38 C
ANISOU 693 CA GLY A 102 1111 1207 1244 -25 -16 -125 C
ATOM 694 C GLY A 102 37.804 45.634 42.802 1.00 8.63 C
ANISOU 694 C GLY A 102 1018 1120 1141 -27 -14 -119 C
ATOM 695 O GLY A 102 37.324 46.754 42.991 1.00 9.56 O
ANISOU 695 O GLY A 102 1139 1239 1255 -29 -19 -108 O
ATOM 696 N ILE A 103 39.025 45.468 42.318 1.00 9.35 N
ANISOU 696 N ILE A 103 1106 1216 1229 -28 -6 -124 N
ATOM 697 CA ILE A 103 39.809 46.555 41.726 1.00 9.68 C
ANISOU 697 CA ILE A 103 1150 1268 1262 -33 -3 -118 C
ATOM 698 C ILE A 103 40.024 46.255 40.247 1.00 9.84 C
ANISOU 698 C ILE A 103 1171 1298 1268 -37 2 -126 C
ATOM 699 O ILE A 103 40.633 45.199 39.908 1.00 11.58 O
ANISOU 699 O ILE A 103 1389 1520 1491 -33 9 -138 O
ATOM 700 CB ILE A 103 41.147 46.809 42.455 1.00 9.73 C
ANISOU 700 CB ILE A 103 1150 1274 1274 -32 2 -115 C
ATOM 701 CG1 ILE A 103 40.865 47.362 43.851 1.00 9.19 C
ANISOU 701 CG1 ILE A 103 1080 1197 1213 -29 -4 -107 C
ATOM 702 CG2 ILE A 103 42.038 47.734 41.646 1.00 9.90 C
ANISOU 702 CG2 ILE A 103 1170 1306 1284 -38 7 -112 C
ATOM 703 CD1 ILE A 103 42.086 47.544 44.750 1.00 9.84 C
ANISOU 703 CD1 ILE A 103 1156 1280 1302 -29 -1 -104 C
ATOM 704 N ARG A 104 39.615 47.186 39.379 1.00 10.77 N
ANISOU 704 N ARG A 104 1294 1424 1373 -42 -1 -120 N
ATOM 705 CA ARG A 104 39.764 47.022 37.939 1.00 11.85 C
ANISOU 705 CA ARG A 104 1434 1573 1495 -46 3 -127 C
ATOM 706 C ARG A 104 41.087 47.587 37.405 1.00 11.79 C
ANISOU 706 C ARG A 104 1425 1576 1481 -49 13 -124 C
ATOM 707 O ARG A 104 41.584 47.123 36.398 1.00 11.87 O
ANISOU 707 O ARG A 104 1435 1595 1482 -50 20 -132 O
ATOM 708 CB ARG A 104 38.637 47.764 37.216 1.00 12.64 C
ANISOU 708 CB ARG A 104 1540 1678 1583 -51 -5 -120 C
ATOM 709 CG ARG A 104 37.191 47.282 37.488 1.00 14.61 C
ANISOU 709 CG ARG A 104 1791 1923 1836 -49 -14 -121 C
ATOM 710 CD ARG A 104 36.988 45.806 37.402 1.00 19.89 C
ANISOU 710 CD ARG A 104 2458 2588 2510 -48 -14 -137 C
ATOM 711 NE ARG A 104 37.046 45.379 36.035 1.00 22.27 N
ANISOU 711 NE ARG A 104 2764 2902 2797 -53 -11 -147 N
ATOM 712 CZ ARG A 104 36.011 44.964 35.292 1.00 23.78 C
ANISOU 712 CZ ARG A 104 2957 3098 2979 -57 -18 -153 C
ATOM 713 NH1 ARG A 104 34.774 44.917 35.758 1.00 24.17 N
ANISOU 713 NH1 ARG A 104 3006 3143 3034 -58 -28 -148 N
ATOM 714 NH2 ARG A 104 36.257 44.563 34.071 1.00 23.11 N
ANISOU 714 NH2 ARG A 104 2877 3025 2880 -61 -15 -163 N
ATOM 715 N ASP A 105 41.571 48.658 38.018 1.00 10.52 N
ANISOU 715 N ASP A 105 1262 1413 1324 -52 12 -112 N
ATOM 716 CA ASP A 105 42.776 49.366 37.563 1.00 10.24 C
ANISOU 716 CA ASP A 105 1223 1385 1281 -57 21 -107 C
ATOM 717 C ASP A 105 43.247 50.270 38.661 1.00 9.68 C
ANISOU 717 C ASP A 105 1151 1308 1220 -60 18 -97 C
ATOM 718 O ASP A 105 42.450 50.649 39.584 1.00 9.02 O
ANISOU 718 O ASP A 105 1070 1213 1143 -58 10 -92 O
ATOM 719 CB ASP A 105 42.391 50.254 36.380 1.00 10.28 C
ANISOU 719 CB ASP A 105 1235 1400 1269 -64 20 -100 C
ATOM 720 CG ASP A 105 43.576 50.740 35.532 1.00 10.80 C
ANISOU 720 CG ASP A 105 1298 1479 1325 -70 31 -96 C
ATOM 721 OD1 ASP A 105 44.706 50.292 35.699 1.00 11.32 O
ANISOU 721 OD1 ASP A 105 1355 1548 1396 -69 39 -101 O
ATOM 722 OD2 ASP A 105 43.282 51.621 34.645 1.00 11.15 O
ANISOU 722 OD2 ASP A 105 1349 1530 1356 -76 30 -87 O
ATOM 723 N ILE A 106 44.521 50.624 38.629 1.00 9.63 N
ANISOU 723 N ILE A 106 1137 1308 1214 -65 26 -94 N
ATOM 724 CA ILE A 106 45.037 51.595 39.553 1.00 9.83 C
ANISOU 724 CA ILE A 106 1162 1328 1246 -70 23 -85 C
ATOM 725 C ILE A 106 45.967 52.516 38.766 1.00 10.05 C
ANISOU 725 C ILE A 106 1188 1366 1265 -81 31 -77 C
ATOM 726 O ILE A 106 46.859 52.013 38.023 1.00 10.45 O
ANISOU 726 O ILE A 106 1230 1430 1310 -81 40 -82 O
ATOM 727 CB ILE A 106 45.804 50.958 40.732 1.00 10.52 C
ANISOU 727 CB ILE A 106 1238 1412 1346 -66 24 -89 C
ATOM 728 CG1 ILE A 106 44.943 49.924 41.506 1.00 10.80 C
ANISOU 728 CG1 ILE A 106 1274 1437 1391 -55 18 -96 C
ATOM 729 CG2 ILE A 106 46.356 52.071 41.616 1.00 10.95 C
ANISOU 729 CG2 ILE A 106 1291 1462 1405 -74 21 -80 C
ATOM 730 CD1 ILE A 106 45.693 49.215 42.593 1.00 11.39 C
ANISOU 730 CD1 ILE A 106 1339 1511 1478 -49 19 -99 C
ATOM 731 N LEU A 107 45.778 53.829 38.925 1.00 10.23 N
ANISOU 731 N LEU A 107 1218 1382 1285 -89 27 -65 N
ATOM 732 CA LEU A 107 46.671 54.830 38.280 1.00 10.71 C
ANISOU 732 CA LEU A 107 1279 1451 1339 -101 33 -56 C
ATOM 733 C LEU A 107 47.524 55.505 39.346 1.00 9.94 C
ANISOU 733 C LEU A 107 1177 1348 1252 -110 32 -51 C
ATOM 734 O LEU A 107 47.024 55.922 40.405 1.00 9.55 O
ANISOU 734 O LEU A 107 1133 1285 1210 -109 24 -50 O
ATOM 735 CB LEU A 107 45.892 55.878 37.486 1.00 11.47 C
ANISOU 735 CB LEU A 107 1388 1545 1425 -106 31 -45 C
ATOM 736 CG LEU A 107 44.968 55.295 36.403 1.00 13.05 C
ANISOU 736 CG LEU A 107 1593 1752 1613 -99 31 -49 C
ATOM 737 CD1 LEU A 107 43.605 54.893 36.971 1.00 14.52 C
ANISOU 737 CD1 LEU A 107 1785 1927 1804 -89 21 -52 C
ATOM 738 CD2 LEU A 107 44.787 56.264 35.224 1.00 13.43 C
ANISOU 738 CD2 LEU A 107 1650 1807 1646 -105 34 -36 C
ATOM 739 N ARG A 108 48.787 55.754 39.036 1.00 9.95 N
ANISOU 739 N ARG A 108 1169 1361 1252 -119 40 -48 N
ATOM 740 CA ARG A 108 49.661 56.546 39.885 1.00 10.25 C
ANISOU 740 CA ARG A 108 1201 1395 1297 -131 38 -43 C
ATOM 741 C ARG A 108 50.895 56.911 39.044 1.00 10.53 C
ANISOU 741 C ARG A 108 1228 1447 1327 -143 49 -37 C
ATOM 742 O ARG A 108 51.075 56.370 37.936 1.00 11.26 O
ANISOU 742 O ARG A 108 1315 1552 1410 -139 58 -39 O
ATOM 743 CB ARG A 108 49.978 55.819 41.217 1.00 10.01 C
ANISOU 743 CB ARG A 108 1161 1362 1279 -125 33 -50 C
ATOM 744 CG ARG A 108 50.568 54.430 41.147 1.00 9.87 C
ANISOU 744 CG ARG A 108 1129 1357 1264 -114 38 -60 C
ATOM 745 CD ARG A 108 52.001 54.408 40.601 1.00 10.30 C
ANISOU 745 CD ARG A 108 1168 1430 1317 -121 49 -57 C
ATOM 746 NE ARG A 108 52.607 53.123 40.817 1.00 10.23 N
ANISOU 746 NE ARG A 108 1144 1431 1314 -109 53 -66 N
ATOM 747 CZ ARG A 108 53.696 52.702 40.152 1.00 11.02 C
ANISOU 747 CZ ARG A 108 1228 1548 1410 -109 65 -66 C
ATOM 748 NH1 ARG A 108 54.278 53.481 39.233 1.00 11.41 N
ANISOU 748 NH1 ARG A 108 1276 1608 1451 -121 73 -59 N
ATOM 749 NH2 ARG A 108 54.223 51.510 40.420 1.00 11.51 N
ANISOU 749 NH2 ARG A 108 1277 1617 1478 -95 69 -74 N
ATOM 750 N ALA A 109 51.683 57.850 39.547 1.00 10.58 N
ANISOU 750 N ALA A 109 1231 1451 1337 -158 48 -30 N
ATOM 751 CA ALA A 109 52.818 58.349 38.820 1.00 10.77 C
ANISOU 751 CA ALA A 109 1246 1489 1357 -172 58 -22 C
ATOM 752 C ALA A 109 53.860 57.318 38.554 1.00 11.50 C
ANISOU 752 C ALA A 109 1318 1602 1450 -167 67 -28 C
ATOM 753 O ALA A 109 53.987 56.362 39.284 1.00 11.20 O
ANISOU 753 O ALA A 109 1271 1566 1419 -156 64 -37 O
ATOM 754 CB ALA A 109 53.422 59.524 39.564 1.00 10.78 C
ANISOU 754 CB ALA A 109 1248 1483 1365 -191 53 -14 C
ATOM 755 N SER A 110 54.698 57.575 37.538 1.00 12.20 N
ANISOU 755 N SER A 110 1398 1706 1530 -175 78 -21 N
ATOM 756 CA SER A 110 55.694 56.565 37.139 1.00 13.38 C
ANISOU 756 CA SER A 110 1528 1877 1679 -168 89 -27 C
ATOM 757 C SER A 110 56.881 56.472 38.076 1.00 13.57 C
ANISOU 757 C SER A 110 1532 1909 1713 -174 88 -26 C
ATOM 758 O SER A 110 57.675 55.533 37.957 1.00 15.56 O
ANISOU 758 O SER A 110 1767 2179 1968 -165 96 -31 O
ATOM 759 CB SER A 110 56.213 56.913 35.754 1.00 14.30 C
ANISOU 759 CB SER A 110 1641 2009 1781 -176 103 -19 C
ATOM 760 OG SER A 110 56.879 58.146 35.763 1.00 15.59 O
ANISOU 760 OG SER A 110 1804 2174 1946 -197 104 -6 O
ATOM 761 N THR A 111 57.085 57.482 38.921 1.00 12.64 N
ANISOU 761 N THR A 111 1417 1783 1603 -191 80 -20 N
ATOM 762 CA THR A 111 58.132 57.432 39.909 1.00 12.96 C
ANISOU 762 CA THR A 111 1439 1832 1654 -198 76 -20 C
ATOM 763 C THR A 111 57.576 57.618 41.330 1.00 12.90 C
ANISOU 763 C THR A 111 1440 1806 1655 -197 60 -24 C
ATOM 764 O THR A 111 56.568 58.316 41.546 1.00 12.39 O
ANISOU 764 O THR A 111 1396 1722 1590 -200 53 -23 O
ATOM 765 CB THR A 111 59.214 58.521 39.682 1.00 13.77 C
ANISOU 765 CB THR A 111 1532 1944 1755 -222 80 -8 C
ATOM 766 OG1 THR A 111 58.614 59.808 39.828 1.00 16.17 O
ANISOU 766 OG1 THR A 111 1856 2228 2058 -238 73 -1 O
ATOM 767 CG2 THR A 111 59.812 58.397 38.284 1.00 14.48 C
ANISOU 767 CG2 THR A 111 1613 2054 1835 -223 97 -2 C
ATOM 768 N LEU A 112 58.295 57.087 42.307 1.00 12.63 N
ANISOU 768 N LEU A 112 1389 1781 1630 -195 56 -28 N
ATOM 769 CA LEU A 112 57.922 57.175 43.693 1.00 13.30 C
ANISOU 769 CA LEU A 112 1479 1853 1722 -194 42 -32 C
ATOM 770 C LEU A 112 57.845 58.634 44.165 1.00 13.16 C
ANISOU 770 C LEU A 112 1474 1821 1704 -217 34 -26 C
ATOM 771 O LEU A 112 56.907 59.023 44.863 1.00 12.20 O
ANISOU 771 O LEU A 112 1371 1681 1585 -215 24 -29 O
ATOM 772 CB LEU A 112 58.935 56.456 44.561 1.00 14.80 C
ANISOU 772 CB LEU A 112 1646 2059 1920 -190 39 -34 C
ATOM 773 CG LEU A 112 58.590 56.284 46.022 1.00 16.10 C
ANISOU 773 CG LEU A 112 1813 2213 2090 -186 25 -39 C
ATOM 774 CD1 LEU A 112 57.644 55.112 46.103 1.00 16.17 C
ANISOU 774 CD1 LEU A 112 1829 2214 2100 -161 25 -47 C
ATOM 775 CD2 LEU A 112 59.846 56.012 46.866 1.00 18.55 C
ANISOU 775 CD2 LEU A 112 2099 2543 2406 -191 21 -37 C
ATOM 776 N GLU A 113 58.823 59.433 43.778 1.00 12.87 N
ANISOU 776 N GLU A 113 1429 1795 1667 -237 38 -18 N
ATOM 777 CA GLU A 113 58.911 60.807 44.204 1.00 12.60 C
ANISOU 777 CA GLU A 113 1406 1748 1634 -261 32 -13 C
ATOM 778 C GLU A 113 57.748 61.656 43.693 1.00 12.34 C
ANISOU 778 C GLU A 113 1401 1691 1596 -262 32 -9 C
ATOM 779 O GLU A 113 57.267 62.532 44.400 1.00 13.51 O
ANISOU 779 O GLU A 113 1566 1820 1747 -271 23 -10 O
ATOM 780 CB GLU A 113 60.271 61.401 43.799 1.00 13.18 C
ANISOU 780 CB GLU A 113 1462 1839 1708 -284 38 -4 C
ATOM 781 CG GLU A 113 60.422 62.858 44.159 1.00 14.18 C
ANISOU 781 CG GLU A 113 1601 1951 1836 -311 32 2 C
ATOM 782 CD GLU A 113 60.661 63.121 45.615 1.00 14.26 C
ANISOU 782 CD GLU A 113 1610 1956 1853 -320 17 -5 C
ATOM 783 OE1 GLU A 113 60.872 62.192 46.463 1.00 13.76 O
ANISOU 783 OE1 GLU A 113 1532 1903 1792 -307 11 -12 O
ATOM 784 OE2 GLU A 113 60.671 64.360 45.904 1.00 15.73 O
ANISOU 784 OE2 GLU A 113 1811 2126 2041 -342 12 -2 O
ATOM 785 N ALA A 114 57.275 61.362 42.498 1.00 12.09 N
ANISOU 785 N ALA A 114 1375 1663 1558 -252 42 -6 N
ATOM 786 CA ALA A 114 56.185 62.068 41.874 1.00 11.84 C
ANISOU 786 CA ALA A 114 1366 1612 1520 -251 42 -2 C
ATOM 787 C ALA A 114 54.844 61.595 42.406 1.00 11.27 C
ANISOU 787 C ALA A 114 1309 1524 1449 -231 35 -10 C
ATOM 788 O ALA A 114 53.857 62.292 42.273 1.00 12.69 O
ANISOU 788 O ALA A 114 1510 1686 1627 -230 32 -6 O
ATOM 789 CB ALA A 114 56.209 61.875 40.361 1.00 12.26 C
ANISOU 789 CB ALA A 114 1417 1677 1562 -247 55 5 C
ATOM 790 N MET A 115 54.799 60.411 42.996 1.00 11.03 N
ANISOU 790 N MET A 115 1267 1501 1422 -215 31 -19 N
ATOM 791 CA MET A 115 53.489 59.810 43.397 1.00 10.55 C
ANISOU 791 CA MET A 115 1219 1427 1362 -195 25 -27 C
ATOM 792 C MET A 115 52.992 60.510 44.671 1.00 10.52 C
ANISOU 792 C MET A 115 1229 1405 1364 -199 14 -29 C
ATOM 793 O MET A 115 53.568 60.377 45.724 1.00 10.17 O
ANISOU 793 O MET A 115 1176 1364 1326 -203 8 -33 O
ATOM 794 CB MET A 115 53.624 58.300 43.615 1.00 10.36 C
ANISOU 794 CB MET A 115 1179 1415 1340 -177 26 -36 C
ATOM 795 CG MET A 115 52.304 57.696 44.073 1.00 10.26 C
ANISOU 795 CG MET A 115 1178 1389 1330 -160 20 -42 C
ATOM 796 SD MET A 115 52.322 55.893 44.163 1.00 10.77 S
ANISOU 796 SD MET A 115 1228 1465 1398 -138 23 -52 S
ATOM 797 CE MET A 115 53.415 55.542 45.541 1.00 10.94 C
ANISOU 797 CE MET A 115 1233 1496 1430 -141 17 -55 C
ATOM 798 N ARG A 116 51.882 61.263 44.520 1.00 10.36 N
ANISOU 798 N ARG A 116 1230 1366 1341 -197 11 -26 N
ATOM 799 CA ARG A 116 51.141 61.874 45.610 1.00 10.93 C
ANISOU 799 CA ARG A 116 1318 1418 1417 -197 2 -28 C
ATOM 800 C ARG A 116 49.740 61.276 45.808 1.00 10.63 C
ANISOU 800 C ARG A 116 1290 1371 1379 -175 -1 -33 C
ATOM 801 O ARG A 116 49.132 61.440 46.891 1.00 10.96 O
ANISOU 801 O ARG A 116 1340 1399 1424 -170 -9 -37 O
ATOM 802 CB ARG A 116 50.972 63.379 45.287 1.00 11.68 C
ANISOU 802 CB ARG A 116 1431 1496 1510 -211 3 -19 C
ATOM 803 CG ARG A 116 52.289 64.101 45.098 1.00 12.71 C
ANISOU 803 CG ARG A 116 1554 1633 1641 -235 7 -14 C
ATOM 804 CD ARG A 116 53.244 63.933 46.290 1.00 13.12 C
ANISOU 804 CD ARG A 116 1594 1692 1700 -245 0 -21 C
ATOM 805 NE ARG A 116 52.620 64.349 47.527 1.00 14.68 N
ANISOU 805 NE ARG A 116 1805 1871 1900 -243 -10 -28 N
ATOM 806 CZ ARG A 116 53.032 64.011 48.739 1.00 16.26 C
ANISOU 806 CZ ARG A 116 1998 2076 2104 -245 -18 -36 C
ATOM 807 NH1 ARG A 116 54.131 63.258 48.909 1.00 17.08 N
ANISOU 807 NH1 ARG A 116 2077 2202 2209 -248 -19 -38 N
ATOM 808 NH2 ARG A 116 52.373 64.466 49.799 1.00 18.39 N
ANISOU 808 NH2 ARG A 116 2284 2329 2375 -242 -26 -42 N
ATOM 809 N ASP A 117 49.240 60.636 44.761 1.00 10.86 N
ANISOU 809 N ASP A 117 1317 1407 1403 -164 4 -31 N
ATOM 810 CA ASP A 117 47.850 60.167 44.653 1.00 10.94 C
ANISOU 810 CA ASP A 117 1336 1410 1412 -147 2 -33 C
ATOM 811 C ASP A 117 47.816 58.785 44.118 1.00 10.75 C
ANISOU 811 C ASP A 117 1299 1400 1386 -135 5 -39 C
ATOM 812 O ASP A 117 48.600 58.455 43.279 1.00 11.18 O
ANISOU 812 O ASP A 117 1343 1469 1437 -139 12 -38 O
ATOM 813 CB ASP A 117 47.073 61.099 43.692 1.00 11.94 C
ANISOU 813 CB ASP A 117 1478 1527 1531 -148 4 -23 C
ATOM 814 CG ASP A 117 47.327 62.546 43.973 1.00 12.15 C
ANISOU 814 CG ASP A 117 1518 1539 1559 -163 4 -16 C
ATOM 815 OD1 ASP A 117 46.976 62.960 45.093 1.00 13.11 O
ANISOU 815 OD1 ASP A 117 1649 1647 1687 -162 -3 -20 O
ATOM 816 OD2 ASP A 117 47.917 63.222 43.140 1.00 13.56 O
ANISOU 816 OD2 ASP A 117 1698 1720 1733 -175 9 -8 O
ATOM 817 N VAL A 118 46.843 57.982 44.578 1.00 9.98 N
ANISOU 817 N VAL A 118 1204 1298 1291 -120 1 -45 N
ATOM 818 CA VAL A 118 46.560 56.698 43.968 1.00 9.92 C
ANISOU 818 CA VAL A 118 1187 1300 1281 -108 4 -51 C
ATOM 819 C VAL A 118 45.119 56.736 43.563 1.00 9.32 C
ANISOU 819 C VAL A 118 1123 1216 1201 -99 1 -49 C
ATOM 820 O VAL A 118 44.248 57.018 44.395 1.00 10.07 O
ANISOU 820 O VAL A 118 1227 1299 1301 -93 -5 -48 O
ATOM 821 CB VAL A 118 46.848 55.512 44.932 1.00 10.95 C
ANISOU 821 CB VAL A 118 1306 1434 1420 -99 2 -60 C
ATOM 822 CG1 VAL A 118 46.581 54.179 44.290 1.00 11.34 C
ANISOU 822 CG1 VAL A 118 1349 1491 1469 -87 6 -66 C
ATOM 823 CG2 VAL A 118 48.290 55.615 45.411 1.00 12.09 C
ANISOU 823 CG2 VAL A 118 1437 1587 1568 -108 3 -60 C
ATOM 824 N TYR A 119 44.827 56.412 42.317 1.00 8.72 N
ANISOU 824 N TYR A 119 1048 1149 1118 -96 5 -49 N
ATOM 825 CA TYR A 119 43.468 56.385 41.797 1.00 8.24 C
ANISOU 825 CA TYR A 119 996 1084 1052 -88 2 -46 C
ATOM 826 C TYR A 119 43.099 54.915 41.642 1.00 8.25 C
ANISOU 826 C TYR A 119 989 1091 1054 -78 2 -57 C
ATOM 827 O TYR A 119 43.706 54.198 40.836 1.00 8.82 O
ANISOU 827 O TYR A 119 1053 1176 1121 -79 8 -62 O
ATOM 828 CB TYR A 119 43.359 57.095 40.459 1.00 8.49 C
ANISOU 828 CB TYR A 119 1033 1121 1071 -94 6 -38 C
ATOM 829 CG TYR A 119 43.696 58.547 40.523 1.00 8.54 C
ANISOU 829 CG TYR A 119 1050 1120 1077 -104 7 -26 C
ATOM 830 CD1 TYR A 119 42.698 59.506 40.818 1.00 8.75 C
ANISOU 830 CD1 TYR A 119 1089 1131 1103 -101 2 -18 C
ATOM 831 CD2 TYR A 119 44.998 59.022 40.240 1.00 9.14 C
ANISOU 831 CD2 TYR A 119 1120 1201 1151 -117 13 -23 C
ATOM 832 CE1 TYR A 119 42.990 60.841 40.855 1.00 8.91 C
ANISOU 832 CE1 TYR A 119 1120 1141 1123 -110 3 -8 C
ATOM 833 CE2 TYR A 119 45.273 60.394 40.261 1.00 9.52 C
ANISOU 833 CE2 TYR A 119 1179 1240 1199 -129 14 -12 C
ATOM 834 CZ TYR A 119 44.283 61.299 40.552 1.00 9.40 C
ANISOU 834 CZ TYR A 119 1179 1208 1185 -125 9 -5 C
ATOM 835 OH TYR A 119 44.557 62.658 40.551 1.00 10.21 O
ANISOU 835 OH TYR A 119 1294 1299 1288 -136 11 6 O
ATOM 836 N ILE A 120 42.032 54.500 42.323 1.00 8.00 N
ANISOU 836 N ILE A 120 959 1051 1027 -69 -5 -59 N
ATOM 837 CA ILE A 120 41.628 53.073 42.297 1.00 8.43 C
ANISOU 837 CA ILE A 120 1008 1110 1085 -60 -5 -70 C
ATOM 838 C ILE A 120 40.307 52.991 41.570 1.00 8.28 C
ANISOU 838 C ILE A 120 995 1092 1060 -56 -9 -68 C
ATOM 839 O ILE A 120 39.324 53.643 41.979 1.00 8.34 O
ANISOU 839 O ILE A 120 1010 1091 1068 -53 -15 -61 O
ATOM 840 CB ILE A 120 41.524 52.536 43.752 1.00 9.05 C
ANISOU 840 CB ILE A 120 1083 1180 1176 -54 -9 -73 C
ATOM 841 CG1 ILE A 120 42.891 52.689 44.466 1.00 9.23 C
ANISOU 841 CG1 ILE A 120 1099 1205 1204 -59 -6 -74 C
ATOM 842 CG2 ILE A 120 41.036 51.101 43.735 1.00 8.99 C
ANISOU 842 CG2 ILE A 120 1070 1173 1172 -46 -9 -82 C
ATOM 843 CD1 ILE A 120 42.883 52.339 45.939 1.00 10.01 C
ANISOU 843 CD1 ILE A 120 1195 1296 1313 -54 -10 -75 C
ATOM 844 N VAL A 121 40.292 52.230 40.486 1.00 8.06 N
ANISOU 844 N VAL A 121 964 1074 1024 -56 -6 -74 N
ATOM 845 CA VAL A 121 39.144 52.126 39.599 1.00 8.08 C
ANISOU 845 CA VAL A 121 972 1082 1018 -54 -10 -74 C
ATOM 846 C VAL A 121 38.398 50.852 39.976 1.00 8.11 C
ANISOU 846 C VAL A 121 971 1081 1028 -48 -14 -83 C
ATOM 847 O VAL A 121 39.037 49.757 40.114 1.00 8.09 O
ANISOU 847 O VAL A 121 963 1081 1032 -47 -10 -94 O
ATOM 848 CB VAL A 121 39.611 52.076 38.105 1.00 8.27 C
ANISOU 848 CB VAL A 121 995 1119 1027 -60 -5 -76 C
ATOM 849 CG1 VAL A 121 38.391 51.986 37.152 1.00 8.29 C
ANISOU 849 CG1 VAL A 121 1003 1129 1018 -58 -11 -75 C
ATOM 850 CG2 VAL A 121 40.509 53.265 37.786 1.00 8.75 C
ANISOU 850 CG2 VAL A 121 1059 1183 1082 -67 1 -65 C
ATOM 851 N GLN A 122 37.074 50.944 40.138 1.00 8.38 N
ANISOU 851 N GLN A 122 1009 1113 1064 -44 -22 -79 N
ATOM 852 CA GLN A 122 36.242 49.853 40.592 1.00 8.34 C
ANISOU 852 CA GLN A 122 999 1103 1065 -40 -26 -86 C
ATOM 853 C GLN A 122 34.916 49.865 39.818 1.00 8.50 C
ANISOU 853 C GLN A 122 1021 1131 1078 -40 -33 -84 C
ATOM 854 O GLN A 122 34.522 50.894 39.211 1.00 9.14 O
ANISOU 854 O GLN A 122 1108 1217 1149 -41 -36 -74 O
ATOM 855 CB GLN A 122 36.004 49.988 42.112 1.00 8.21 C
ANISOU 855 CB GLN A 122 982 1076 1063 -34 -28 -82 C
ATOM 856 CG GLN A 122 37.319 50.005 42.907 1.00 8.24 C
ANISOU 856 CG GLN A 122 982 1074 1073 -35 -23 -84 C
ATOM 857 CD GLN A 122 37.101 50.099 44.410 1.00 8.42 C
ANISOU 857 CD GLN A 122 1005 1087 1108 -29 -25 -81 C
ATOM 858 OE1 GLN A 122 36.909 51.189 44.942 1.00 8.34 O
ANISOU 858 OE1 GLN A 122 1000 1072 1097 -29 -28 -72 O
ATOM 859 NE2 GLN A 122 37.198 48.975 45.090 1.00 9.11 N
ANISOU 859 NE2 GLN A 122 1087 1171 1204 -25 -25 -87 N
ATOM 860 N ASP A 123 34.199 48.757 39.874 1.00 9.11 N
ANISOU 860 N ASP A 123 1095 1208 1159 -39 -37 -92 N
ATOM 861 CA ASP A 123 32.879 48.690 39.254 1.00 9.67 C
ANISOU 861 CA ASP A 123 1166 1286 1224 -41 -45 -90 C
ATOM 862 C ASP A 123 31.993 49.799 39.790 1.00 9.88 C
ANISOU 862 C ASP A 123 1192 1309 1251 -35 -50 -74 C
ATOM 863 O ASP A 123 31.944 50.018 41.018 1.00 9.15 O
ANISOU 863 O ASP A 123 1100 1206 1170 -30 -49 -70 O
ATOM 864 CB ASP A 123 32.226 47.310 39.512 1.00 10.88 C
ANISOU 864 CB ASP A 123 1313 1435 1384 -42 -48 -101 C
ATOM 865 CG ASP A 123 32.905 46.180 38.811 1.00 11.85 C
ANISOU 865 CG ASP A 123 1437 1561 1505 -47 -43 -117 C
ATOM 866 OD1 ASP A 123 33.616 46.379 37.790 1.00 13.79 O
ANISOU 866 OD1 ASP A 123 1686 1816 1738 -50 -39 -121 O
ATOM 867 OD2 ASP A 123 32.683 45.029 39.332 1.00 14.06 O
ANISOU 867 OD2 ASP A 123 1714 1832 1796 -47 -43 -126 O
ATOM 868 N LEU A 124 31.227 50.435 38.913 1.00 9.55 N
ANISOU 868 N LEU A 124 1153 1279 1198 -36 -55 -66 N
ATOM 869 CA LEU A 124 30.233 51.435 39.295 1.00 10.25 C
ANISOU 869 CA LEU A 124 1242 1366 1287 -29 -61 -51 C
ATOM 870 C LEU A 124 28.956 50.777 39.762 1.00 10.95 C
ANISOU 870 C LEU A 124 1324 1456 1383 -26 -67 -51 C
ATOM 871 O LEU A 124 28.404 49.927 39.036 1.00 13.03 O
ANISOU 871 O LEU A 124 1582 1729 1641 -32 -73 -59 O
ATOM 872 CB LEU A 124 29.996 52.405 38.128 1.00 10.33 C
ANISOU 872 CB LEU A 124 1257 1387 1282 -29 -63 -41 C
ATOM 873 CG LEU A 124 29.086 53.590 38.413 1.00 10.53 C
ANISOU 873 CG LEU A 124 1284 1409 1306 -20 -67 -23 C
ATOM 874 CD1 LEU A 124 29.648 54.463 39.515 1.00 10.68 C
ANISOU 874 CD1 LEU A 124 1310 1412 1335 -15 -61 -18 C
ATOM 875 CD2 LEU A 124 28.857 54.360 37.150 1.00 11.74 C
ANISOU 875 CD2 LEU A 124 1441 1575 1443 -21 -70 -13 C
ATOM 876 N MET A 125 28.489 51.120 40.954 1.00 10.43 N
ANISOU 876 N MET A 125 1255 1379 1327 -18 -67 -44 N
ATOM 877 CA MET A 125 27.223 50.647 41.488 1.00 10.37 C
ANISOU 877 CA MET A 125 1240 1374 1327 -14 -73 -41 C
ATOM 878 C MET A 125 26.245 51.807 41.525 1.00 10.56 C
ANISOU 878 C MET A 125 1264 1401 1348 -5 -76 -25 C
ATOM 879 O MET A 125 26.552 52.917 41.064 1.00 11.30 O
ANISOU 879 O MET A 125 1365 1495 1433 -2 -75 -16 O
ATOM 880 CB MET A 125 27.455 50.028 42.879 1.00 10.47 C
ANISOU 880 CB MET A 125 1250 1373 1354 -11 -68 -46 C
ATOM 881 CG MET A 125 28.494 48.920 42.849 1.00 11.41 C
ANISOU 881 CG MET A 125 1370 1488 1478 -19 -64 -61 C
ATOM 882 SD MET A 125 27.984 47.424 42.109 1.00 12.48 S
ANISOU 882 SD MET A 125 1498 1630 1612 -28 -68 -73 S
ATOM 883 CE MET A 125 27.038 46.745 43.454 1.00 13.19 C
ANISOU 883 CE MET A 125 1580 1712 1718 -24 -70 -70 C
ATOM 884 N GLU A 126 25.012 51.539 41.933 1.00 11.06 N
ANISOU 884 N GLU A 126 1318 1469 1415 -1 -81 -20 N
ATOM 885 CA GLU A 126 23.962 52.558 41.830 1.00 11.86 C
ANISOU 885 CA GLU A 126 1417 1576 1513 10 -85 -3 C
ATOM 886 C GLU A 126 23.819 53.343 43.130 1.00 10.87 C
ANISOU 886 C GLU A 126 1296 1438 1397 23 -80 5 C
ATOM 887 O GLU A 126 23.532 54.523 43.135 1.00 10.70 O
ANISOU 887 O GLU A 126 1280 1414 1372 33 -78 17 O
ATOM 888 CB GLU A 126 22.667 51.839 41.539 1.00 13.96 C
ANISOU 888 CB GLU A 126 1669 1857 1779 7 -94 -2 C
ATOM 889 CG GLU A 126 21.440 52.711 41.463 1.00 18.25 C
ANISOU 889 CG GLU A 126 2206 2409 2319 19 -98 16 C
ATOM 890 CD GLU A 126 21.398 53.560 40.218 1.00 23.69 C
ANISOU 890 CD GLU A 126 2899 3109 2993 20 -103 24 C
ATOM 891 OE1 GLU A 126 22.227 53.356 39.308 1.00 27.75 O
ANISOU 891 OE1 GLU A 126 3420 3627 3498 10 -103 16 O
ATOM 892 OE2 GLU A 126 20.511 54.449 40.169 1.00 33.34 O
ANISOU 892 OE2 GLU A 126 4118 4337 4213 32 -105 41 O
ATOM 893 N THR A 127 23.980 52.670 44.242 1.00 9.69 N
ANISOU 893 N THR A 127 1143 1279 1258 23 -76 -2 N
ATOM 894 CA THR A 127 23.743 53.273 45.514 1.00 9.73 C
ANISOU 894 CA THR A 127 1152 1273 1271 34 -71 5 C
ATOM 895 C THR A 127 24.481 52.504 46.599 1.00 9.33 C
ANISOU 895 C THR A 127 1102 1212 1230 31 -66 -5 C
ATOM 896 O THR A 127 25.252 51.571 46.294 1.00 8.85 O
ANISOU 896 O THR A 127 1040 1151 1171 21 -66 -17 O
ATOM 897 CB THR A 127 22.216 53.358 45.800 1.00 10.00 C
ANISOU 897 CB THR A 127 1175 1316 1308 44 -74 16 C
ATOM 898 OG1 THR A 127 21.984 54.238 46.905 1.00 10.94 O
ANISOU 898 OG1 THR A 127 1300 1426 1432 58 -68 24 O
ATOM 899 CG2 THR A 127 21.610 51.976 46.077 1.00 9.92 C
ANISOU 899 CG2 THR A 127 1151 1313 1306 37 -77 10 C
ATOM 900 N ASP A 128 24.200 52.870 47.848 1.00 9.24 N
ANISOU 900 N ASP A 128 1093 1193 1226 41 -61 -1 N
ATOM 901 CA ASP A 128 24.630 52.044 48.978 1.00 9.04 C
ANISOU 901 CA ASP A 128 1066 1161 1210 40 -57 -8 C
ATOM 902 C ASP A 128 23.511 51.866 49.963 1.00 8.60 C
ANISOU 902 C ASP A 128 1003 1106 1160 49 -56 -1 C
ATOM 903 O ASP A 128 22.451 52.473 49.830 1.00 9.33 O
ANISOU 903 O ASP A 128 1091 1205 1251 58 -57 10 O
ATOM 904 CB ASP A 128 25.929 52.596 49.580 1.00 9.49 C
ANISOU 904 CB ASP A 128 1135 1205 1266 40 -52 -13 C
ATOM 905 CG ASP A 128 25.768 53.952 50.216 1.00 10.27 C
ANISOU 905 CG ASP A 128 1243 1296 1362 51 -49 -5 C
ATOM 906 OD1 ASP A 128 24.833 54.093 51.015 1.00 11.02 O
ANISOU 906 OD1 ASP A 128 1336 1391 1461 61 -47 1 O
ATOM 907 OD2 ASP A 128 26.579 54.878 49.931 1.00 11.91 O
ANISOU 907 OD2 ASP A 128 1462 1497 1565 49 -47 -6 O
ATOM 908 N LEU A 129 23.676 50.932 50.886 1.00 8.09 N
ANISOU 908 N LEU A 129 933 1037 1102 47 -53 -6 N
ATOM 909 CA LEU A 129 22.553 50.613 51.765 1.00 8.43 C
ANISOU 909 CA LEU A 129 967 1084 1152 54 -51 2 C
ATOM 910 C LEU A 129 22.203 51.759 52.709 1.00 8.54 C
ANISOU 910 C LEU A 129 987 1092 1164 70 -46 10 C
ATOM 911 O LEU A 129 21.052 51.865 53.161 1.00 9.48 O
ANISOU 911 O LEU A 129 1099 1218 1286 79 -44 19 O
ATOM 912 CB LEU A 129 22.855 49.376 52.595 1.00 8.27 C
ANISOU 912 CB LEU A 129 942 1059 1140 49 -49 -4 C
ATOM 913 CG LEU A 129 21.659 48.820 53.437 1.00 8.65 C
ANISOU 913 CG LEU A 129 979 1112 1195 54 -47 4 C
ATOM 914 CD1 LEU A 129 20.497 48.335 52.597 1.00 9.00 C
ANISOU 914 CD1 LEU A 129 1009 1169 1241 48 -53 9 C
ATOM 915 CD2 LEU A 129 22.135 47.682 54.326 1.00 8.72 C
ANISOU 915 CD2 LEU A 129 986 1114 1212 49 -43 0 C
ATOM 916 N TYR A 130 23.161 52.605 53.048 1.00 8.88 N
ANISOU 916 N TYR A 130 1045 1126 1204 72 -43 7 N
ATOM 917 CA TYR A 130 22.837 53.794 53.855 1.00 9.66 C
ANISOU 917 CA TYR A 130 1153 1219 1300 87 -37 13 C
ATOM 918 C TYR A 130 21.844 54.675 53.120 1.00 9.89 C
ANISOU 918 C TYR A 130 1180 1253 1325 96 -39 24 C
ATOM 919 O TYR A 130 20.800 55.064 53.651 1.00 9.67 O
ANISOU 919 O TYR A 130 1148 1228 1298 109 -35 33 O
ATOM 920 CB TYR A 130 24.110 54.566 54.192 1.00 9.92 C
ANISOU 920 CB TYR A 130 1202 1238 1329 85 -35 6 C
ATOM 921 CG TYR A 130 23.887 55.852 54.939 1.00 10.79 C
ANISOU 921 CG TYR A 130 1325 1340 1436 98 -29 10 C
ATOM 922 CD1 TYR A 130 23.835 55.858 56.299 1.00 10.85 C
ANISOU 922 CD1 TYR A 130 1335 1342 1444 105 -24 9 C
ATOM 923 CD2 TYR A 130 23.694 57.038 54.280 1.00 11.33 C
ANISOU 923 CD2 TYR A 130 1402 1404 1500 103 -29 16 C
ATOM 924 CE1 TYR A 130 23.639 57.024 57.011 1.00 12.24 C
ANISOU 924 CE1 TYR A 130 1525 1510 1616 117 -18 11 C
ATOM 925 CE2 TYR A 130 23.461 58.193 54.973 1.00 12.03 C
ANISOU 925 CE2 TYR A 130 1503 1482 1585 116 -23 19 C
ATOM 926 CZ TYR A 130 23.360 58.150 56.320 1.00 12.69 C
ANISOU 926 CZ TYR A 130 1591 1562 1671 124 -18 16 C
ATOM 927 OH TYR A 130 23.193 59.312 57.062 1.00 14.32 O
ANISOU 927 OH TYR A 130 1811 1756 1873 136 -11 17 O
ATOM 928 N LYS A 131 22.170 54.987 51.888 1.00 9.70 N
ANISOU 928 N LYS A 131 1159 1231 1296 89 -43 23 N
ATOM 929 CA LYS A 131 21.288 55.842 51.053 1.00 10.27 C
ANISOU 929 CA LYS A 131 1229 1310 1363 98 -46 35 C
ATOM 930 C LYS A 131 19.941 55.154 50.876 1.00 10.08 C
ANISOU 930 C LYS A 131 1187 1302 1342 101 -50 43 C
ATOM 931 O LYS A 131 18.871 55.812 50.971 1.00 11.44 O
ANISOU 931 O LYS A 131 1354 1479 1514 115 -48 55 O
ATOM 932 CB LYS A 131 21.965 56.204 49.723 1.00 10.76 C
ANISOU 932 CB LYS A 131 1298 1373 1419 89 -50 33 C
ATOM 933 CG LYS A 131 23.241 57.029 49.938 1.00 12.03 C
ANISOU 933 CG LYS A 131 1476 1518 1577 86 -46 28 C
ATOM 934 CD LYS A 131 23.779 57.745 48.702 1.00 14.10 C
ANISOU 934 CD LYS A 131 1747 1780 1831 81 -49 31 C
ATOM 935 CE LYS A 131 24.420 56.832 47.770 1.00 13.83 C
ANISOU 935 CE LYS A 131 1706 1754 1793 65 -53 23 C
ATOM 936 NZ LYS A 131 25.100 57.531 46.583 1.00 13.90 N
ANISOU 936 NZ LYS A 131 1724 1763 1794 59 -55 25 N
ATOM 937 N LEU A 132 19.941 53.847 50.627 1.00 10.13 N
ANISOU 937 N LEU A 132 1181 1316 1352 87 -54 36 N
ATOM 938 CA LEU A 132 18.723 53.167 50.362 1.00 10.31 C
ANISOU 938 CA LEU A 132 1186 1353 1377 87 -59 42 C
ATOM 939 C LEU A 132 17.795 53.175 51.581 1.00 10.08 C
ANISOU 939 C LEU A 132 1150 1326 1355 99 -52 51 C
ATOM 940 O LEU A 132 16.574 53.395 51.453 1.00 10.58 O
ANISOU 940 O LEU A 132 1200 1401 1417 108 -54 62 O
ATOM 941 CB LEU A 132 18.990 51.763 49.859 1.00 11.12 C
ANISOU 941 CB LEU A 132 1281 1461 1483 68 -64 32 C
ATOM 942 CG LEU A 132 17.834 50.921 49.452 1.00 12.12 C
ANISOU 942 CG LEU A 132 1389 1603 1612 62 -71 36 C
ATOM 943 CD1 LEU A 132 17.057 51.571 48.313 1.00 13.37 C
ANISOU 943 CD1 LEU A 132 1541 1777 1763 65 -78 46 C
ATOM 944 CD2 LEU A 132 18.359 49.553 49.052 1.00 12.83 C
ANISOU 944 CD2 LEU A 132 1476 1692 1706 43 -75 23 C
ATOM 945 N LEU A 133 18.338 52.929 52.765 1.00 9.57 N
ANISOU 945 N LEU A 133 1091 1250 1294 101 -46 45 N
ATOM 946 CA LEU A 133 17.528 52.894 54.002 1.00 9.84 C
ANISOU 946 CA LEU A 133 1119 1286 1333 113 -38 52 C
ATOM 947 C LEU A 133 17.047 54.278 54.400 1.00 10.83 C
ANISOU 947 C LEU A 133 1252 1409 1455 133 -32 61 C
ATOM 948 O LEU A 133 16.025 54.387 55.102 1.00 11.58 O
ANISOU 948 O LEU A 133 1338 1510 1552 146 -27 71 O
ATOM 949 CB LEU A 133 18.289 52.252 55.138 1.00 10.10 C
ANISOU 949 CB LEU A 133 1158 1309 1370 109 -33 44 C
ATOM 950 CG LEU A 133 18.492 50.781 54.909 1.00 9.68 C
ANISOU 950 CG LEU A 133 1095 1260 1324 92 -37 38 C
ATOM 951 CD1 LEU A 133 19.322 50.249 56.097 1.00 10.56 C
ANISOU 951 CD1 LEU A 133 1214 1361 1439 91 -32 32 C
ATOM 952 CD2 LEU A 133 17.203 49.997 54.775 1.00 10.92 C
ANISOU 952 CD2 LEU A 133 1233 1431 1487 89 -40 46 C
ATOM 953 N LYS A 134 17.707 55.365 53.987 1.00 10.71 N
ANISOU 953 N LYS A 134 1253 1383 1433 137 -32 59 N
ATOM 954 CA LYS A 134 17.100 56.680 54.197 1.00 11.86 C
ANISOU 954 CA LYS A 134 1406 1526 1576 157 -26 69 C
ATOM 955 C LYS A 134 15.914 56.905 53.291 1.00 12.85 C
ANISOU 955 C LYS A 134 1516 1666 1700 164 -31 83 C
ATOM 956 O LYS A 134 14.972 57.636 53.696 1.00 14.31 O
ANISOU 956 O LYS A 134 1698 1854 1885 183 -25 94 O
ATOM 957 CB LYS A 134 18.107 57.787 54.004 1.00 11.09 C
ANISOU 957 CB LYS A 134 1330 1411 1473 158 -24 64 C
ATOM 958 CG LYS A 134 19.240 57.769 55.022 1.00 12.04 C
ANISOU 958 CG LYS A 134 1465 1516 1593 153 -19 52 C
ATOM 959 CD LYS A 134 18.747 58.029 56.404 1.00 13.27 C
ANISOU 959 CD LYS A 134 1624 1669 1750 168 -10 53 C
ATOM 960 CE LYS A 134 19.906 58.112 57.412 1.00 14.81 C
ANISOU 960 CE LYS A 134 1834 1850 1943 163 -6 41 C
ATOM 961 NZ LYS A 134 19.388 58.419 58.781 1.00 17.58 N
ANISOU 961 NZ LYS A 134 2189 2197 2292 178 3 42 N
ATOM 962 N SER A 135 15.927 56.254 52.140 1.00 13.50 N
ANISOU 962 N SER A 135 1589 1760 1781 149 -41 82 N
ATOM 963 CA ASER A 135 14.945 56.521 51.067 0.50 14.66 C
ANISOU 963 CA ASER A 135 1723 1924 1925 154 -48 94 C
ATOM 964 CA BSER A 135 14.945 56.543 51.073 0.50 14.69 C
ANISOU 964 CA BSER A 135 1726 1926 1927 154 -48 95 C
ATOM 965 C SER A 135 13.699 55.688 51.190 1.00 15.68 C
ANISOU 965 C SER A 135 1828 2072 2059 153 -51 102 C
ATOM 966 O SER A 135 12.635 56.082 50.746 1.00 19.04 O
ANISOU 966 O SER A 135 2240 2511 2482 164 -53 116 O
ATOM 967 CB ASER A 135 15.549 56.222 49.704 0.50 14.91 C
ANISOU 967 CB ASER A 135 1755 1959 1950 137 -58 89 C
ATOM 968 CB BSER A 135 15.577 56.397 49.666 0.50 15.08 C
ANISOU 968 CB BSER A 135 1780 1980 1971 139 -57 90 C
ATOM 969 OG ASER A 135 14.583 56.446 48.691 0.50 16.38 O
ANISOU 969 OG ASER A 135 1929 2163 2131 141 -66 101 O
ATOM 970 OG BSER A 135 15.788 55.057 49.267 0.50 15.93 O
ANISOU 970 OG BSER A 135 1877 2095 2080 119 -64 80 O
ATOM 971 N GLN A 136 13.792 54.493 51.709 1.00 15.11 N
ANISOU 971 N GLN A 136 1748 2000 1992 140 -51 94 N
ATOM 972 CA GLN A 136 12.590 53.656 51.739 1.00 15.86 C
ANISOU 972 CA GLN A 136 1819 2115 2093 137 -54 102 C
ATOM 973 C GLN A 136 12.665 52.511 52.705 1.00 14.40 C
ANISOU 973 C GLN A 136 1628 1927 1916 127 -50 96 C
ATOM 974 O GLN A 136 13.742 52.030 53.072 1.00 13.53 O
ANISOU 974 O GLN A 136 1530 1802 1807 118 -48 83 O
ATOM 975 CB GLN A 136 12.295 53.089 50.359 1.00 18.57 C
ANISOU 975 CB GLN A 136 2150 2473 2432 121 -68 102 C
ATOM 976 CG GLN A 136 13.333 52.075 49.941 1.00 20.33 C
ANISOU 976 CG GLN A 136 2380 2689 2656 99 -73 85 C
ATOM 977 CD GLN A 136 12.998 51.373 48.623 1.00 25.91 C
ANISOU 977 CD GLN A 136 3074 3411 3358 82 -86 82 C
ATOM 978 OE1 GLN A 136 13.366 51.849 47.570 1.00 28.46 O
ANISOU 978 OE1 GLN A 136 3405 3737 3673 80 -92 81 O
ATOM 979 NE2 GLN A 136 12.339 50.195 48.700 1.00 28.82 N
ANISOU 979 NE2 GLN A 136 3427 3791 3734 68 -90 81 N
ATOM 980 N GLN A 137 11.499 52.039 53.087 1.00 13.73 N
ANISOU 980 N GLN A 137 1523 1856 1836 130 -49 106 N
ATOM 981 CA GLN A 137 11.337 50.832 53.810 1.00 14.54 C
ANISOU 981 CA GLN A 137 1617 1961 1948 118 -47 103 C
ATOM 982 C GLN A 137 11.533 49.690 52.834 1.00 14.16 C
ANISOU 982 C GLN A 137 1562 1917 1902 94 -58 94 C
ATOM 983 O GLN A 137 11.095 49.746 51.687 1.00 16.42 O
ANISOU 983 O GLN A 137 1840 2217 2184 88 -68 96 O
ATOM 984 CB GLN A 137 9.932 50.776 54.363 1.00 15.84 C
ANISOU 984 CB GLN A 137 1760 2143 2117 128 -42 118 C
ATOM 985 CG GLN A 137 9.679 49.592 55.196 1.00 18.15 C
ANISOU 985 CG GLN A 137 2043 2436 2419 117 -38 118 C
ATOM 986 CD GLN A 137 8.385 49.750 55.919 1.00 22.85 C
ANISOU 986 CD GLN A 137 2618 3046 3016 131 -31 134 C
ATOM 987 OE1 GLN A 137 7.366 50.062 55.302 1.00 26.39 O
ANISOU 987 OE1 GLN A 137 3050 3514 3465 135 -36 146 O
ATOM 988 NE2 GLN A 137 8.451 49.688 57.274 1.00 22.61 N
ANISOU 988 NE2 GLN A 137 2592 3009 2989 140 -18 136 N
ATOM 989 N LEU A 138 12.284 48.707 53.249 1.00 13.27 N
ANISOU 989 N LEU A 138 1455 1792 1794 80 -57 83 N
ATOM 990 CA LEU A 138 12.498 47.491 52.434 1.00 13.20 C
ANISOU 990 CA LEU A 138 1441 1785 1789 57 -66 73 C
ATOM 991 C LEU A 138 11.472 46.450 52.729 1.00 13.36 C
ANISOU 991 C LEU A 138 1442 1816 1818 46 -67 79 C
ATOM 992 O LEU A 138 11.087 46.251 53.887 1.00 14.44 O
ANISOU 992 O LEU A 138 1574 1952 1962 53 -58 86 O
ATOM 993 CB LEU A 138 13.884 46.887 52.769 1.00 13.15 C
ANISOU 993 CB LEU A 138 1452 1758 1785 49 -62 58 C
ATOM 994 CG LEU A 138 15.053 47.778 52.368 1.00 13.41 C
ANISOU 994 CG LEU A 138 1505 1781 1809 55 -62 50 C
ATOM 995 CD1 LEU A 138 16.311 47.027 52.782 1.00 13.02 C
ANISOU 995 CD1 LEU A 138 1468 1715 1764 46 -59 37 C
ATOM 996 CD2 LEU A 138 15.028 48.200 50.889 1.00 14.28 C
ANISOU 996 CD2 LEU A 138 1616 1901 1911 49 -72 48 C
ATOM 997 N SER A 139 11.135 45.681 51.688 1.00 13.04 N
ANISOU 997 N SER A 139 1392 1785 1778 27 -78 74 N
ATOM 998 CA SER A 139 10.294 44.509 51.899 1.00 13.48 C
ANISOU 998 CA SER A 139 1429 1847 1843 11 -80 77 C
ATOM 999 C SER A 139 11.086 43.473 52.669 1.00 12.96 C
ANISOU 999 C SER A 139 1373 1762 1787 2 -74 67 C
ATOM 1000 O SER A 139 12.322 43.442 52.608 1.00 12.49 O
ANISOU 1000 O SER A 139 1333 1687 1725 2 -72 55 O
ATOM 1001 CB SER A 139 9.842 43.889 50.557 1.00 14.90 C
ANISOU 1001 CB SER A 139 1599 2040 2021 -9 -95 71 C
ATOM 1002 OG SER A 139 10.917 43.342 49.880 1.00 15.63 O
ANISOU 1002 OG SER A 139 1708 2120 2112 -22 -99 53 O
ATOM 1003 N ASN A 140 10.393 42.517 53.261 1.00 12.58 N
ANISOU 1003 N ASN A 140 1313 1718 1751 -8 -71 73 N
ATOM 1004 CA ASN A 140 11.057 41.329 53.874 1.00 12.28 C
ANISOU 1004 CA ASN A 140 1283 1661 1722 -19 -66 65 C
ATOM 1005 C ASN A 140 11.903 40.593 52.838 1.00 12.57 C
ANISOU 1005 C ASN A 140 1331 1686 1758 -37 -74 47 C
ATOM 1006 O ASN A 140 12.988 40.094 53.192 1.00 12.17 O
ANISOU 1006 O ASN A 140 1296 1617 1712 -38 -69 37 O
ATOM 1007 CB ASN A 140 10.023 40.373 54.475 1.00 13.07 C
ANISOU 1007 CB ASN A 140 1364 1766 1834 -31 -63 75 C
ATOM 1008 CG ASN A 140 10.642 39.255 55.242 1.00 13.00 C
ANISOU 1008 CG ASN A 140 1365 1739 1836 -39 -56 71 C
ATOM 1009 OD1 ASN A 140 11.490 39.474 56.112 1.00 13.43 O
ANISOU 1009 OD1 ASN A 140 1432 1780 1889 -26 -47 70 O
ATOM 1010 ND2 ASN A 140 10.259 38.027 54.908 1.00 14.05 N
ANISOU 1010 ND2 ASN A 140 1490 1869 1979 -62 -61 67 N
ATOM 1011 N ASP A 141 11.453 40.493 51.592 1.00 13.00 N
ANISOU 1011 N ASP A 141 1378 1753 1808 -50 -86 42 N
ATOM 1012 CA ASP A 141 12.231 39.808 50.537 1.00 13.00 C
ANISOU 1012 CA ASP A 141 1390 1743 1806 -66 -93 23 C
ATOM 1013 C ASP A 141 13.585 40.499 50.387 1.00 12.86 C
ANISOU 1013 C ASP A 141 1393 1714 1780 -54 -89 14 C
ATOM 1014 O ASP A 141 14.607 39.832 50.240 1.00 11.74 O
ANISOU 1014 O ASP A 141 1265 1556 1641 -60 -87 1 O
ATOM 1015 CB ASP A 141 11.529 39.854 49.139 1.00 14.49 C
ANISOU 1015 CB ASP A 141 1569 1951 1987 -80 -107 19 C
ATOM 1016 CG ASP A 141 10.189 39.091 49.041 1.00 17.67 C
ANISOU 1016 CG ASP A 141 1949 2367 2396 -97 -114 26 C
ATOM 1017 OD1 ASP A 141 9.960 38.007 49.579 1.00 15.02 O
ANISOU 1017 OD1 ASP A 141 1610 2023 2073 -110 -111 25 O
ATOM 1018 OD2 ASP A 141 9.397 39.561 48.156 1.00 23.83 O
ANISOU 1018 OD2 ASP A 141 2716 3169 3167 -100 -125 30 O
ATOM 1019 N HIS A 142 13.573 41.821 50.339 1.00 12.31 N
ANISOU 1019 N HIS A 142 1325 1653 1700 -37 -89 22 N
ATOM 1020 CA HIS A 142 14.815 42.555 50.075 1.00 12.79 C
ANISOU 1020 CA HIS A 142 1404 1704 1752 -27 -86 14 C
ATOM 1021 C HIS A 142 15.753 42.501 51.285 1.00 11.23 C
ANISOU 1021 C HIS A 142 1218 1489 1561 -17 -75 13 C
ATOM 1022 O HIS A 142 16.959 42.368 51.120 1.00 10.52 O
ANISOU 1022 O HIS A 142 1142 1386 1469 -18 -73 2 O
ATOM 1023 CB HIS A 142 14.557 43.984 49.673 1.00 14.77 C
ANISOU 1023 CB HIS A 142 1654 1966 1991 -12 -89 23 C
ATOM 1024 CG HIS A 142 14.029 44.098 48.281 1.00 19.72 C
ANISOU 1024 CG HIS A 142 2274 2610 2609 -21 -101 21 C
ATOM 1025 ND1 HIS A 142 14.807 43.850 47.174 1.00 26.14 N
ANISOU 1025 ND1 HIS A 142 3097 3420 3415 -32 -107 7 N
ATOM 1026 CD2 HIS A 142 12.782 44.315 47.815 1.00 23.53 C
ANISOU 1026 CD2 HIS A 142 2740 3113 3089 -23 -109 31 C
ATOM 1027 CE1 HIS A 142 14.072 43.957 46.083 1.00 25.62 C
ANISOU 1027 CE1 HIS A 142 3021 3372 3340 -40 -118 8 C
ATOM 1028 NE2 HIS A 142 12.851 44.283 46.445 1.00 27.61 N
ANISOU 1028 NE2 HIS A 142 3257 3639 3595 -34 -120 24 N
ATOM 1029 N ILE A 143 15.204 42.622 52.462 1.00 10.78 N
ANISOU 1029 N ILE A 143 1154 1432 1509 -7 -68 25 N
ATOM 1030 CA ILE A 143 15.978 42.466 53.698 1.00 10.58 C
ANISOU 1030 CA ILE A 143 1138 1392 1488 1 -58 25 C
ATOM 1031 C ILE A 143 16.677 41.130 53.705 1.00 10.34 C
ANISOU 1031 C ILE A 143 1114 1348 1468 -13 -57 15 C
ATOM 1032 O ILE A 143 17.915 41.072 53.912 1.00 9.98 O
ANISOU 1032 O ILE A 143 1082 1289 1421 -10 -53 6 O
ATOM 1033 CB ILE A 143 15.084 42.604 54.946 1.00 10.99 C
ANISOU 1033 CB ILE A 143 1180 1449 1545 11 -50 41 C
ATOM 1034 CG1 ILE A 143 14.530 44.063 55.020 1.00 11.94 C
ANISOU 1034 CG1 ILE A 143 1298 1581 1656 29 -49 51 C
ATOM 1035 CG2 ILE A 143 15.872 42.280 56.203 1.00 11.19 C
ANISOU 1035 CG2 ILE A 143 1216 1462 1576 18 -40 41 C
ATOM 1036 CD1 ILE A 143 13.453 44.176 56.063 1.00 12.99 C
ANISOU 1036 CD1 ILE A 143 1418 1723 1793 39 -41 66 C
ATOM 1037 N CYS A 144 15.924 40.079 53.412 1.00 9.86 N
ANISOU 1037 N CYS A 144 1042 1289 1414 -29 -61 14 N
ATOM 1038 CA CYS A 144 16.427 38.708 53.478 1.00 9.69 C
ANISOU 1038 CA CYS A 144 1026 1253 1404 -42 -59 5 C
ATOM 1039 C CYS A 144 17.521 38.536 52.443 1.00 9.30 C
ANISOU 1039 C CYS A 144 990 1195 1349 -48 -63 -12 C
ATOM 1040 O CYS A 144 18.568 37.973 52.704 1.00 9.17 O
ANISOU 1040 O CYS A 144 984 1163 1336 -47 -58 -19 O
ATOM 1041 CB CYS A 144 15.272 37.746 53.196 1.00 9.45 C
ANISOU 1041 CB CYS A 144 981 1228 1382 -60 -64 8 C
ATOM 1042 SG CYS A 144 15.654 36.037 53.492 1.00 10.93 S
ANISOU 1042 SG CYS A 144 1174 1395 1585 -76 -60 1 S
ATOM 1043 N TYR A 145 17.273 38.980 51.228 1.00 9.05 N
ANISOU 1043 N TYR A 145 957 1175 1309 -53 -72 -17 N
ATOM 1044 CA TYR A 145 18.214 38.787 50.130 1.00 9.26 C
ANISOU 1044 CA TYR A 145 995 1196 1329 -60 -76 -34 C
ATOM 1045 C TYR A 145 19.489 39.622 50.313 1.00 8.78 C
ANISOU 1045 C TYR A 145 947 1128 1260 -46 -70 -37 C
ATOM 1046 O TYR A 145 20.602 39.178 49.998 1.00 9.59 O
ANISOU 1046 O TYR A 145 1061 1221 1364 -48 -68 -49 O
ATOM 1047 CB TYR A 145 17.550 39.131 48.806 1.00 9.90 C
ANISOU 1047 CB TYR A 145 1069 1293 1399 -69 -86 -37 C
ATOM 1048 CG TYR A 145 18.385 38.811 47.600 1.00 11.20 C
ANISOU 1048 CG TYR A 145 1246 1455 1557 -78 -90 -55 C
ATOM 1049 CD1 TYR A 145 18.844 37.534 47.378 1.00 11.17 C
ANISOU 1049 CD1 TYR A 145 1247 1436 1560 -90 -89 -69 C
ATOM 1050 CD2 TYR A 145 18.683 39.811 46.651 1.00 11.83 C
ANISOU 1050 CD2 TYR A 145 1329 1545 1620 -73 -95 -57 C
ATOM 1051 CE1 TYR A 145 19.637 37.240 46.282 1.00 12.89 C
ANISOU 1051 CE1 TYR A 145 1477 1651 1771 -97 -91 -86 C
ATOM 1052 CE2 TYR A 145 19.430 39.503 45.549 1.00 13.57 C
ANISOU 1052 CE2 TYR A 145 1559 1763 1833 -81 -98 -73 C
ATOM 1053 CZ TYR A 145 19.906 38.239 45.383 1.00 13.67 C
ANISOU 1053 CZ TYR A 145 1579 1763 1853 -92 -95 -87 C
ATOM 1054 OH TYR A 145 20.623 37.946 44.255 1.00 17.38 O
ANISOU 1054 OH TYR A 145 2058 2231 2314 -99 -97 -103 O
ATOM 1055 N PHE A 146 19.347 40.885 50.738 1.00 8.20 N
ANISOU 1055 N PHE A 146 873 1063 1181 -31 -69 -26 N
ATOM 1056 CA PHE A 146 20.545 41.676 51.067 1.00 8.40 C
ANISOU 1056 CA PHE A 146 911 1081 1200 -19 -64 -28 C
ATOM 1057 C PHE A 146 21.368 41.010 52.164 1.00 8.40 C
ANISOU 1057 C PHE A 146 917 1067 1209 -15 -56 -29 C
ATOM 1058 O PHE A 146 22.599 40.924 52.105 1.00 8.81 O
ANISOU 1058 O PHE A 146 978 1109 1260 -13 -53 -38 O
ATOM 1059 CB PHE A 146 20.197 43.106 51.437 1.00 9.05 C
ANISOU 1059 CB PHE A 146 992 1171 1274 -4 -63 -17 C
ATOM 1060 CG PHE A 146 19.738 43.965 50.277 1.00 9.53 C
ANISOU 1060 CG PHE A 146 1051 1246 1325 -5 -70 -15 C
ATOM 1061 CD1 PHE A 146 20.289 43.835 49.038 1.00 9.81 C
ANISOU 1061 CD1 PHE A 146 1092 1283 1353 -14 -75 -26 C
ATOM 1062 CD2 PHE A 146 18.788 44.945 50.472 1.00 10.48 C
ANISOU 1062 CD2 PHE A 146 1165 1377 1441 6 -71 -2 C
ATOM 1063 CE1 PHE A 146 19.888 44.650 48.021 1.00 11.97 C
ANISOU 1063 CE1 PHE A 146 1363 1569 1615 -13 -82 -23 C
ATOM 1064 CE2 PHE A 146 18.348 45.711 49.446 1.00 11.65 C
ANISOU 1064 CE2 PHE A 146 1310 1537 1579 7 -77 1 C
ATOM 1065 CZ PHE A 146 18.927 45.594 48.225 1.00 11.80 C
ANISOU 1065 CZ PHE A 146 1335 1558 1591 -3 -83 -9 C
ATOM 1066 N LEU A 147 20.699 40.526 53.206 1.00 8.05 N
ANISOU 1066 N LEU A 147 864 1020 1173 -14 -52 -20 N
ATOM 1067 CA LEU A 147 21.372 39.806 54.283 1.00 8.22 C
ANISOU 1067 CA LEU A 147 890 1028 1203 -10 -44 -19 C
ATOM 1068 C LEU A 147 22.118 38.617 53.758 1.00 8.12 C
ANISOU 1068 C LEU A 147 884 1004 1198 -20 -44 -31 C
ATOM 1069 O LEU A 147 23.274 38.360 54.126 1.00 7.78 O
ANISOU 1069 O LEU A 147 848 950 1156 -15 -40 -36 O
ATOM 1070 CB LEU A 147 20.390 39.419 55.392 1.00 9.20 C
ANISOU 1070 CB LEU A 147 1005 1155 1336 -8 -40 -5 C
ATOM 1071 CG LEU A 147 21.034 38.675 56.607 1.00 10.26 C
ANISOU 1071 CG LEU A 147 1144 1277 1479 -3 -32 -2 C
ATOM 1072 CD1 LEU A 147 22.046 39.598 57.312 1.00 11.14 C
ANISOU 1072 CD1 LEU A 147 1265 1386 1581 11 -29 -1 C
ATOM 1073 CD2 LEU A 147 20.003 38.144 57.614 1.00 10.85 C
ANISOU 1073 CD2 LEU A 147 1209 1354 1561 -4 -27 12 C
ATOM 1074 N TYR A 148 21.453 37.847 52.924 1.00 8.48 N
ANISOU 1074 N TYR A 148 924 1050 1247 -35 -49 -37 N
ATOM 1075 CA TYR A 148 22.097 36.673 52.311 1.00 8.15 C
ANISOU 1075 CA TYR A 148 889 996 1212 -45 -49 -50 C
ATOM 1076 C TYR A 148 23.431 37.075 51.614 1.00 8.04 C
ANISOU 1076 C TYR A 148 886 979 1189 -40 -48 -62 C
ATOM 1077 O TYR A 148 24.454 36.460 51.800 1.00 8.22 O
ANISOU 1077 O TYR A 148 916 990 1217 -38 -43 -68 O
ATOM 1078 CB TYR A 148 21.138 36.016 51.298 1.00 8.59 C
ANISOU 1078 CB TYR A 148 939 1055 1269 -63 -56 -57 C
ATOM 1079 CG TYR A 148 21.827 34.941 50.521 1.00 8.36 C
ANISOU 1079 CG TYR A 148 920 1014 1245 -73 -55 -74 C
ATOM 1080 CD1 TYR A 148 22.214 33.775 51.156 1.00 8.34 C
ANISOU 1080 CD1 TYR A 148 921 991 1255 -75 -49 -75 C
ATOM 1081 CD2 TYR A 148 22.213 35.137 49.221 1.00 8.03 C
ANISOU 1081 CD2 TYR A 148 883 976 1192 -78 -60 -88 C
ATOM 1082 CE1 TYR A 148 22.884 32.759 50.473 1.00 8.41 C
ANISOU 1082 CE1 TYR A 148 940 987 1269 -82 -47 -91 C
ATOM 1083 CE2 TYR A 148 22.915 34.168 48.520 1.00 8.18 C
ANISOU 1083 CE2 TYR A 148 912 982 1214 -86 -58 -104 C
ATOM 1084 CZ TYR A 148 23.246 32.962 49.129 1.00 8.25 C
ANISOU 1084 CZ TYR A 148 926 972 1238 -87 -51 -106 C
ATOM 1085 OH TYR A 148 23.988 31.994 48.460 1.00 8.93 O
ANISOU 1085 OH TYR A 148 1022 1043 1327 -93 -48 -123 O
ATOM 1086 N GLN A 149 23.377 38.117 50.786 1.00 7.90 N
ANISOU 1086 N GLN A 149 869 974 1159 -39 -53 -64 N
ATOM 1087 CA GLN A 149 24.566 38.552 50.059 1.00 7.89 C
ANISOU 1087 CA GLN A 149 877 973 1149 -36 -53 -74 C
ATOM 1088 C GLN A 149 25.649 39.067 50.978 1.00 7.42 C
ANISOU 1088 C GLN A 149 822 907 1089 -23 -46 -70 C
ATOM 1089 O GLN A 149 26.851 38.852 50.705 1.00 7.24 O
ANISOU 1089 O GLN A 149 807 879 1066 -21 -43 -79 O
ATOM 1090 CB GLN A 149 24.176 39.590 49.032 1.00 8.02 C
ANISOU 1090 CB GLN A 149 892 1004 1151 -38 -59 -75 C
ATOM 1091 CG GLN A 149 23.296 39.009 47.907 1.00 8.88 C
ANISOU 1091 CG GLN A 149 997 1120 1258 -53 -67 -82 C
ATOM 1092 CD GLN A 149 23.023 40.097 46.898 1.00 9.70 C
ANISOU 1092 CD GLN A 149 1100 1240 1347 -53 -74 -81 C
ATOM 1093 OE1 GLN A 149 23.840 40.399 46.039 1.00 10.01 O
ANISOU 1093 OE1 GLN A 149 1146 1281 1377 -53 -74 -89 O
ATOM 1094 NE2 GLN A 149 21.933 40.724 47.046 1.00 11.18 N
ANISOU 1094 NE2 GLN A 149 1278 1438 1532 -50 -78 -69 N
ATOM 1095 N ILE A 150 25.293 39.798 52.025 1.00 7.39 N
ANISOU 1095 N ILE A 150 816 908 1085 -14 -45 -58 N
ATOM 1096 CA ILE A 150 26.296 40.245 53.006 1.00 7.58 C
ANISOU 1096 CA ILE A 150 845 927 1109 -3 -40 -54 C
ATOM 1097 C ILE A 150 27.009 39.044 53.560 1.00 7.48 C
ANISOU 1097 C ILE A 150 833 901 1106 -2 -34 -57 C
ATOM 1098 O ILE A 150 28.242 39.019 53.641 1.00 7.69 O
ANISOU 1098 O ILE A 150 866 925 1133 2 -31 -62 O
ATOM 1099 CB ILE A 150 25.636 41.023 54.160 1.00 7.95 C
ANISOU 1099 CB ILE A 150 889 979 1155 7 -38 -40 C
ATOM 1100 CG1 ILE A 150 25.024 42.364 53.651 1.00 8.20 C
ANISOU 1100 CG1 ILE A 150 920 1021 1175 10 -42 -37 C
ATOM 1101 CG2 ILE A 150 26.647 41.309 55.244 1.00 8.30 C
ANISOU 1101 CG2 ILE A 150 938 1018 1198 17 -34 -38 C
ATOM 1102 CD1 ILE A 150 24.064 42.999 54.646 1.00 8.34 C
ANISOU 1102 CD1 ILE A 150 933 1044 1193 19 -40 -24 C
ATOM 1103 N LEU A 151 26.247 38.050 53.964 1.00 7.82 N
ANISOU 1103 N LEU A 151 872 939 1159 -7 -33 -53 N
ATOM 1104 CA LEU A 151 26.802 36.828 54.592 1.00 7.99 C
ANISOU 1104 CA LEU A 151 896 947 1193 -6 -28 -53 C
ATOM 1105 C LEU A 151 27.604 35.982 53.585 1.00 8.38 C
ANISOU 1105 C LEU A 151 951 988 1246 -11 -27 -68 C
ATOM 1106 O LEU A 151 28.634 35.385 53.935 1.00 8.18 O
ANISOU 1106 O LEU A 151 929 952 1225 -5 -21 -70 O
ATOM 1107 CB LEU A 151 25.733 36.015 55.298 1.00 8.83 C
ANISOU 1107 CB LEU A 151 996 1048 1310 -10 -26 -44 C
ATOM 1108 CG LEU A 151 25.120 36.679 56.549 1.00 9.05 C
ANISOU 1108 CG LEU A 151 1019 1084 1336 -1 -24 -28 C
ATOM 1109 CD1 LEU A 151 23.838 35.917 56.885 1.00 10.66 C
ANISOU 1109 CD1 LEU A 151 1214 1286 1549 -9 -23 -20 C
ATOM 1110 CD2 LEU A 151 26.123 36.659 57.688 1.00 9.37 C
ANISOU 1110 CD2 LEU A 151 1063 1119 1376 11 -19 -23 C
ATOM 1111 N ARG A 152 27.117 35.898 52.354 1.00 8.29 N
ANISOU 1111 N ARG A 152 939 979 1230 -22 -31 -78 N
ATOM 1112 CA ARG A 152 27.821 35.182 51.341 1.00 8.26 C
ANISOU 1112 CA ARG A 152 942 968 1227 -28 -30 -93 C
ATOM 1113 C ARG A 152 29.238 35.807 51.084 1.00 8.34 C
ANISOU 1113 C ARG A 152 958 983 1230 -18 -27 -98 C
ATOM 1114 O ARG A 152 30.265 35.131 51.038 1.00 8.66 O
ANISOU 1114 O ARG A 152 1002 1013 1274 -14 -21 -104 O
ATOM 1115 CB ARG A 152 26.984 35.137 50.031 1.00 8.59 C
ANISOU 1115 CB ARG A 152 983 1017 1263 -42 -37 -102 C
ATOM 1116 CG ARG A 152 27.578 34.332 48.913 1.00 8.95 C
ANISOU 1116 CG ARG A 152 1037 1056 1308 -48 -35 -120 C
ATOM 1117 CD ARG A 152 26.615 34.221 47.785 1.00 9.41 C
ANISOU 1117 CD ARG A 152 1094 1122 1361 -63 -43 -128 C
ATOM 1118 NE ARG A 152 27.113 33.459 46.643 1.00 10.00 N
ANISOU 1118 NE ARG A 152 1177 1190 1432 -71 -41 -147 N
ATOM 1119 CZ ARG A 152 27.389 33.968 45.464 1.00 11.53 C
ANISOU 1119 CZ ARG A 152 1374 1395 1611 -74 -44 -157 C
ATOM 1120 NH1 ARG A 152 27.426 35.282 45.230 1.00 12.22 N
ANISOU 1120 NH1 ARG A 152 1458 1499 1686 -69 -48 -150 N
ATOM 1121 NH2 ARG A 152 27.627 33.120 44.457 1.00 12.46 N
ANISOU 1121 NH2 ARG A 152 1501 1508 1728 -82 -43 -175 N
ATOM 1122 N GLY A 153 29.279 37.143 50.977 1.00 8.08 N
ANISOU 1122 N GLY A 153 923 962 1184 -15 -30 -94 N
ATOM 1123 CA GLY A 153 30.540 37.867 50.875 1.00 8.16 C
ANISOU 1123 CA GLY A 153 937 977 1188 -8 -28 -96 C
ATOM 1124 C GLY A 153 31.405 37.666 52.098 1.00 7.60 C
ANISOU 1124 C GLY A 153 865 899 1123 3 -23 -89 C
ATOM 1125 O GLY A 153 32.621 37.401 51.984 1.00 7.29 O
ANISOU 1125 O GLY A 153 827 857 1084 7 -18 -94 O
ATOM 1126 N LEU A 154 30.787 37.726 53.276 1.00 7.43 N
ANISOU 1126 N LEU A 154 840 876 1106 7 -23 -77 N
ATOM 1127 CA LEU A 154 31.543 37.588 54.489 1.00 7.57 C
ANISOU 1127 CA LEU A 154 857 890 1127 17 -19 -70 C
ATOM 1128 C LEU A 154 32.097 36.193 54.645 1.00 7.64 C
ANISOU 1128 C LEU A 154 866 886 1148 19 -14 -72 C
ATOM 1129 O LEU A 154 33.158 36.009 55.212 1.00 8.42 O
ANISOU 1129 O LEU A 154 966 984 1250 28 -11 -70 O
ATOM 1130 CB LEU A 154 30.662 37.944 55.703 1.00 7.59 C
ANISOU 1130 CB LEU A 154 857 896 1131 21 -20 -56 C
ATOM 1131 CG LEU A 154 31.454 38.154 57.006 1.00 7.79 C
ANISOU 1131 CG LEU A 154 882 922 1156 31 -18 -48 C
ATOM 1132 CD1 LEU A 154 32.458 39.249 56.935 1.00 8.04 C
ANISOU 1132 CD1 LEU A 154 916 962 1178 34 -20 -51 C
ATOM 1133 CD2 LEU A 154 30.476 38.436 58.131 1.00 8.18 C
ANISOU 1133 CD2 LEU A 154 929 974 1205 35 -18 -36 C
ATOM 1134 N LYS A 155 31.394 35.162 54.178 1.00 7.92 N
ANISOU 1134 N LYS A 155 904 913 1193 12 -13 -77 N
ATOM 1135 CA LYS A 155 31.933 33.795 54.233 1.00 8.66 C
ANISOU 1135 CA LYS A 155 1001 992 1299 14 -7 -81 C
ATOM 1136 C LYS A 155 33.259 33.750 53.458 1.00 8.51 C
ANISOU 1136 C LYS A 155 984 973 1276 19 -3 -92 C
ATOM 1137 O LYS A 155 34.231 33.165 53.904 1.00 8.92 O
ANISOU 1137 O LYS A 155 1037 1019 1335 28 2 -90 O
ATOM 1138 CB LYS A 155 30.918 32.796 53.646 1.00 9.18 C
ANISOU 1138 CB LYS A 155 1068 1046 1373 2 -7 -86 C
ATOM 1139 CG LYS A 155 31.437 31.384 53.637 1.00 10.02 C
ANISOU 1139 CG LYS A 155 1180 1135 1493 4 0 -91 C
ATOM 1140 CD LYS A 155 30.641 30.414 52.773 1.00 10.70 C
ANISOU 1140 CD LYS A 155 1271 1209 1586 -10 0 -102 C
ATOM 1141 CE LYS A 155 31.183 28.996 52.875 1.00 11.26 C
ANISOU 1141 CE LYS A 155 1350 1258 1672 -6 8 -106 C
ATOM 1142 NZ LYS A 155 30.495 28.154 51.903 1.00 12.35 N
ANISOU 1142 NZ LYS A 155 1493 1385 1814 -21 7 -120 N
ATOM 1143 N TYR A 156 33.295 34.374 52.292 1.00 8.12 N
ANISOU 1143 N TYR A 156 937 932 1217 12 -6 -102 N
ATOM 1144 CA TYR A 156 34.507 34.419 51.487 1.00 8.06 C
ANISOU 1144 CA TYR A 156 931 926 1204 16 -2 -113 C
ATOM 1145 C TYR A 156 35.614 35.147 52.256 1.00 8.10 C
ANISOU 1145 C TYR A 156 932 941 1206 26 -1 -105 C
ATOM 1146 O TYR A 156 36.753 34.650 52.351 1.00 8.34 O
ANISOU 1146 O TYR A 156 961 967 1240 35 5 -106 O
ATOM 1147 CB TYR A 156 34.230 35.050 50.122 1.00 8.43 C
ANISOU 1147 CB TYR A 156 981 984 1239 6 -6 -123 C
ATOM 1148 CG TYR A 156 35.407 35.152 49.230 1.00 8.63 C
ANISOU 1148 CG TYR A 156 1008 1014 1258 9 -1 -133 C
ATOM 1149 CD1 TYR A 156 35.811 34.089 48.422 1.00 9.22 C
ANISOU 1149 CD1 TYR A 156 1087 1079 1336 9 5 -147 C
ATOM 1150 CD2 TYR A 156 36.165 36.295 49.231 1.00 8.68 C
ANISOU 1150 CD2 TYR A 156 1011 1033 1255 12 -2 -130 C
ATOM 1151 CE1 TYR A 156 36.877 34.249 47.555 1.00 9.35 C
ANISOU 1151 CE1 TYR A 156 1105 1102 1345 12 10 -156 C
ATOM 1152 CE2 TYR A 156 37.269 36.423 48.365 1.00 9.44 C
ANISOU 1152 CE2 TYR A 156 1107 1135 1344 14 3 -138 C
ATOM 1153 CZ TYR A 156 37.583 35.408 47.543 1.00 9.56 C
ANISOU 1153 CZ TYR A 156 1127 1143 1362 14 9 -151 C
ATOM 1154 OH TYR A 156 38.687 35.590 46.720 1.00 11.48 O
ANISOU 1154 OH TYR A 156 1370 1395 1598 17 15 -159 O
ATOM 1155 N ILE A 157 35.306 36.334 52.770 1.00 7.64 N
ANISOU 1155 N ILE A 157 871 893 1139 25 -7 -96 N
ATOM 1156 CA ILE A 157 36.265 37.146 53.507 1.00 7.67 C
ANISOU 1156 CA ILE A 157 872 906 1138 32 -7 -89 C
ATOM 1157 C ILE A 157 36.844 36.371 54.698 1.00 7.10 C
ANISOU 1157 C ILE A 157 796 827 1076 43 -4 -81 C
ATOM 1158 O ILE A 157 38.087 36.236 54.864 1.00 7.43 O
ANISOU 1158 O ILE A 157 833 871 1117 50 -1 -81 O
ATOM 1159 CB ILE A 157 35.629 38.466 53.933 1.00 7.89 C
ANISOU 1159 CB ILE A 157 899 942 1157 29 -13 -82 C
ATOM 1160 CG1 ILE A 157 35.195 39.309 52.735 1.00 7.91 C
ANISOU 1160 CG1 ILE A 157 904 951 1149 21 -16 -89 C
ATOM 1161 CG2 ILE A 157 36.551 39.267 54.813 1.00 7.98 C
ANISOU 1161 CG2 ILE A 157 908 961 1163 35 -14 -76 C
ATOM 1162 CD1 ILE A 157 34.286 40.441 53.111 1.00 8.36 C
ANISOU 1162 CD1 ILE A 157 963 1015 1200 19 -22 -82 C
ATOM 1163 N HIS A 158 35.949 35.832 55.512 1.00 7.14 N
ANISOU 1163 N HIS A 158 801 824 1087 44 -4 -73 N
ATOM 1164 CA HIS A 158 36.358 35.027 56.699 1.00 7.44 C
ANISOU 1164 CA HIS A 158 837 856 1134 54 -1 -63 C
ATOM 1165 C HIS A 158 37.141 33.789 56.313 1.00 7.96 C
ANISOU 1165 C HIS A 158 903 911 1211 60 6 -68 C
ATOM 1166 O HIS A 158 37.997 33.349 57.101 1.00 8.33 O
ANISOU 1166 O HIS A 158 947 957 1262 71 9 -60 O
ATOM 1167 CB HIS A 158 35.157 34.696 57.553 1.00 7.40 C
ANISOU 1167 CB HIS A 158 832 846 1135 53 -2 -53 C
ATOM 1168 CG HIS A 158 34.738 35.844 58.424 1.00 7.62 C
ANISOU 1168 CG HIS A 158 858 884 1152 54 -7 -44 C
ATOM 1169 ND1 HIS A 158 33.729 35.738 59.369 1.00 7.82 N
ANISOU 1169 ND1 HIS A 158 883 909 1180 54 -7 -33 N
ATOM 1170 CD2 HIS A 158 35.134 37.154 58.448 1.00 7.79 C
ANISOU 1170 CD2 HIS A 158 879 919 1161 53 -11 -45 C
ATOM 1171 CE1 HIS A 158 33.578 36.900 59.975 1.00 8.06 C
ANISOU 1171 CE1 HIS A 158 913 950 1199 56 -10 -28 C
ATOM 1172 NE2 HIS A 158 34.435 37.776 59.448 1.00 7.78 N
ANISOU 1172 NE2 HIS A 158 878 922 1155 55 -13 -36 N
ATOM 1173 N SER A 159 36.857 33.203 55.133 1.00 8.45 N
ANISOU 1173 N SER A 159 970 964 1276 54 9 -80 N
ATOM 1174 CA SER A 159 37.564 31.984 54.714 1.00 9.02 C
ANISOU 1174 CA SER A 159 1045 1024 1358 60 17 -87 C
ATOM 1175 C SER A 159 39.048 32.265 54.473 1.00 9.43 C
ANISOU 1175 C SER A 159 1093 1086 1407 69 20 -90 C
ATOM 1176 O SER A 159 39.859 31.325 54.512 1.00 11.90 O
ANISOU 1176 O SER A 159 1404 1389 1727 80 27 -91 O
ATOM 1177 CB SER A 159 36.908 31.361 53.478 1.00 9.11 C
ANISOU 1177 CB SER A 159 1064 1025 1373 50 19 -102 C
ATOM 1178 OG SER A 159 37.219 32.085 52.341 1.00 9.82 O
ANISOU 1178 OG SER A 159 1154 1126 1450 44 17 -113 O
ATOM 1179 N ALA A 160 39.404 33.541 54.234 1.00 9.62 N
ANISOU 1179 N ALA A 160 1112 1126 1417 66 15 -91 N
ATOM 1180 CA ALA A 160 40.830 33.943 54.119 1.00 9.57 C
ANISOU 1180 CA ALA A 160 1100 1132 1407 73 18 -92 C
ATOM 1181 C ALA A 160 41.433 34.368 55.461 1.00 9.88 C
ANISOU 1181 C ALA A 160 1130 1179 1444 81 14 -78 C
ATOM 1182 O ALA A 160 42.512 34.917 55.526 1.00 9.90 O
ANISOU 1182 O ALA A 160 1126 1195 1441 84 14 -76 O
ATOM 1183 CB ALA A 160 40.951 35.060 53.096 1.00 9.54 C
ANISOU 1183 CB ALA A 160 1095 1140 1389 63 15 -100 C
ATOM 1184 N ASN A 161 40.657 34.171 56.526 1.00 9.50 N
ANISOU 1184 N ASN A 161 1084 1126 1400 82 11 -67 N
ATOM 1185 CA ASN A 161 40.926 34.652 57.883 1.00 10.18 C
ANISOU 1185 CA ASN A 161 1165 1222 1483 87 6 -54 C
ATOM 1186 C ASN A 161 41.029 36.160 57.978 1.00 9.25 C
ANISOU 1186 C ASN A 161 1046 1119 1351 80 -1 -54 C
ATOM 1187 O ASN A 161 41.592 36.684 58.934 1.00 9.92 O
ANISOU 1187 O ASN A 161 1126 1214 1430 83 -5 -46 O
ATOM 1188 CB ASN A 161 42.112 33.974 58.518 1.00 10.94 C
ANISOU 1188 CB ASN A 161 1254 1320 1585 101 9 -46 C
ATOM 1189 CG ASN A 161 41.875 32.534 58.722 1.00 13.46 C
ANISOU 1189 CG ASN A 161 1576 1621 1918 110 16 -42 C
ATOM 1190 OD1 ASN A 161 40.703 32.047 58.851 1.00 15.14 O
ANISOU 1190 OD1 ASN A 161 1795 1821 2136 105 17 -41 O
ATOM 1191 ND2 ASN A 161 42.959 31.788 58.754 1.00 16.24 N
ANISOU 1191 ND2 ASN A 161 1922 1972 2276 123 21 -40 N
ATOM 1192 N VAL A 162 40.387 36.883 57.064 1.00 8.51 N
ANISOU 1192 N VAL A 162 957 1026 1250 69 -3 -63 N
ATOM 1193 CA VAL A 162 40.347 38.348 57.051 1.00 8.06 C
ANISOU 1193 CA VAL A 162 901 982 1182 61 -9 -63 C
ATOM 1194 C VAL A 162 39.090 38.758 57.822 1.00 7.75 C
ANISOU 1194 C VAL A 162 866 939 1139 59 -13 -57 C
ATOM 1195 O VAL A 162 38.005 38.200 57.644 1.00 7.87 O
ANISOU 1195 O VAL A 162 885 945 1160 57 -12 -57 O
ATOM 1196 CB VAL A 162 40.340 38.886 55.589 1.00 8.06 C
ANISOU 1196 CB VAL A 162 904 984 1176 52 -8 -75 C
ATOM 1197 CG1 VAL A 162 40.066 40.368 55.569 1.00 8.21 C
ANISOU 1197 CG1 VAL A 162 925 1010 1183 44 -14 -74 C
ATOM 1198 CG2 VAL A 162 41.653 38.571 54.925 1.00 8.55 C
ANISOU 1198 CG2 VAL A 162 960 1051 1239 55 -3 -80 C
ATOM 1199 N LEU A 163 39.285 39.786 58.641 1.00 7.43 N
ANISOU 1199 N LEU A 163 825 908 1090 58 -18 -52 N
ATOM 1200 CA LEU A 163 38.242 40.459 59.367 1.00 7.82 C
ANISOU 1200 CA LEU A 163 880 958 1135 57 -22 -47 C
ATOM 1201 C LEU A 163 38.045 41.783 58.676 1.00 7.90 C
ANISOU 1201 C LEU A 163 894 972 1135 48 -25 -52 C
ATOM 1202 O LEU A 163 38.991 42.522 58.504 1.00 8.50 O
ANISOU 1202 O LEU A 163 970 1055 1205 45 -27 -55 O
ATOM 1203 CB LEU A 163 38.692 40.705 60.794 1.00 8.18 C
ANISOU 1203 CB LEU A 163 923 1010 1176 63 -25 -38 C
ATOM 1204 CG LEU A 163 39.231 39.476 61.519 1.00 9.04 C
ANISOU 1204 CG LEU A 163 1026 1116 1292 72 -22 -31 C
ATOM 1205 CD1 LEU A 163 39.700 39.894 62.919 1.00 9.40 C
ANISOU 1205 CD1 LEU A 163 1070 1172 1331 77 -26 -22 C
ATOM 1206 CD2 LEU A 163 38.141 38.399 61.636 1.00 9.59 C
ANISOU 1206 CD2 LEU A 163 1098 1174 1372 75 -17 -26 C
ATOM 1207 N HIS A 164 36.812 42.135 58.348 1.00 7.45 N
ANISOU 1207 N HIS A 164 842 911 1076 45 -25 -52 N
ATOM 1208 CA HIS A 164 36.534 43.395 57.706 1.00 7.57 C
ANISOU 1208 CA HIS A 164 863 931 1083 38 -28 -56 C
ATOM 1209 C HIS A 164 36.706 44.569 58.715 1.00 8.07 C
ANISOU 1209 C HIS A 164 931 999 1138 39 -31 -52 C
ATOM 1210 O HIS A 164 37.338 45.614 58.446 1.00 8.25 O
ANISOU 1210 O HIS A 164 956 1025 1153 34 -34 -56 O
ATOM 1211 CB HIS A 164 35.124 43.397 57.081 1.00 7.40 C
ANISOU 1211 CB HIS A 164 844 905 1063 35 -28 -56 C
ATOM 1212 CG HIS A 164 34.783 44.647 56.361 1.00 7.59 C
ANISOU 1212 CG HIS A 164 874 933 1078 30 -30 -58 C
ATOM 1213 ND1 HIS A 164 34.471 45.813 57.023 1.00 7.76 N
ANISOU 1213 ND1 HIS A 164 901 955 1093 32 -32 -54 N
ATOM 1214 CD2 HIS A 164 34.682 44.920 55.041 1.00 7.97 C
ANISOU 1214 CD2 HIS A 164 923 982 1123 24 -31 -64 C
ATOM 1215 CE1 HIS A 164 34.168 46.754 56.135 1.00 7.62 C
ANISOU 1215 CE1 HIS A 164 888 939 1069 28 -34 -56 C
ATOM 1216 NE2 HIS A 164 34.283 46.228 54.929 1.00 7.71 N
ANISOU 1216 NE2 HIS A 164 896 951 1082 23 -33 -61 N
ATOM 1217 N ARG A 165 35.978 44.435 59.829 1.00 8.70 N
ANISOU 1217 N ARG A 165 1012 1077 1218 45 -31 -45 N
ATOM 1218 CA ARG A 165 36.031 45.321 61.006 1.00 9.79 C
ANISOU 1218 CA ARG A 165 1154 1218 1347 48 -34 -42 C
ATOM 1219 C ARG A 165 35.397 46.680 60.826 1.00 10.31 C
ANISOU 1219 C ARG A 165 1229 1283 1405 46 -35 -44 C
ATOM 1220 O ARG A 165 35.482 47.486 61.766 1.00 12.14 O
ANISOU 1220 O ARG A 165 1466 1517 1629 47 -37 -43 O
ATOM 1221 CB ARG A 165 37.464 45.506 61.492 1.00 10.06 C
ANISOU 1221 CB ARG A 165 1186 1259 1377 47 -37 -44 C
ATOM 1222 CG ARG A 165 38.102 44.206 61.941 1.00 10.99 C
ANISOU 1222 CG ARG A 165 1295 1379 1503 53 -36 -39 C
ATOM 1223 CD ARG A 165 39.571 44.273 62.223 1.00 12.35 C
ANISOU 1223 CD ARG A 165 1461 1559 1672 51 -39 -41 C
ATOM 1224 NE ARG A 165 39.848 44.819 63.571 1.00 16.17 N
ANISOU 1224 NE ARG A 165 1947 2050 2147 53 -43 -37 N
ATOM 1225 CZ ARG A 165 40.395 45.983 63.796 1.00 17.50 C
ANISOU 1225 CZ ARG A 165 2120 2224 2305 46 -48 -41 C
ATOM 1226 NH1 ARG A 165 40.647 46.376 65.029 1.00 21.70 N
ANISOU 1226 NH1 ARG A 165 2654 2762 2828 48 -53 -39 N
ATOM 1227 NH2 ARG A 165 40.677 46.759 62.818 1.00 21.82 N
ANISOU 1227 NH2 ARG A 165 2669 2769 2851 37 -48 -48 N
ATOM 1228 N ASP A 166 34.699 46.943 59.725 1.00 9.22 N
ANISOU 1228 N ASP A 166 1093 1142 1268 42 -34 -46 N
ATOM 1229 CA ASP A 166 33.973 48.218 59.642 1.00 9.27 C
ANISOU 1229 CA ASP A 166 1107 1147 1267 42 -35 -45 C
ATOM 1230 C ASP A 166 32.723 48.055 58.829 1.00 8.11 C
ANISOU 1230 C ASP A 166 960 999 1124 43 -33 -43 C
ATOM 1231 O ASP A 166 32.365 48.970 58.030 1.00 8.42 O
ANISOU 1231 O ASP A 166 1003 1036 1158 41 -34 -44 O
ATOM 1232 CB ASP A 166 34.866 49.341 59.123 1.00 9.77 C
ANISOU 1232 CB ASP A 166 1177 1210 1324 35 -37 -50 C
ATOM 1233 CG ASP A 166 34.409 50.726 59.546 1.00 10.62 C
ANISOU 1233 CG ASP A 166 1297 1315 1425 37 -38 -50 C
ATOM 1234 OD1 ASP A 166 33.553 50.927 60.425 1.00 10.13 O
ANISOU 1234 OD1 ASP A 166 1238 1250 1360 45 -36 -46 O
ATOM 1235 OD2 ASP A 166 35.011 51.698 58.966 1.00 11.93 O
ANISOU 1235 OD2 ASP A 166 1469 1479 1586 29 -39 -53 O
ATOM 1236 N LEU A 167 32.022 46.918 58.967 1.00 7.74 N
ANISOU 1236 N LEU A 167 905 951 1084 46 -32 -39 N
ATOM 1237 CA LEU A 167 30.766 46.696 58.234 1.00 8.20 C
ANISOU 1237 CA LEU A 167 959 1009 1146 46 -31 -36 C
ATOM 1238 C LEU A 167 29.701 47.650 58.734 1.00 8.36 C
ANISOU 1238 C LEU A 167 985 1031 1162 52 -30 -30 C
ATOM 1239 O LEU A 167 29.498 47.822 59.954 1.00 8.38 O
ANISOU 1239 O LEU A 167 989 1033 1161 60 -28 -26 O
ATOM 1240 CB LEU A 167 30.297 45.235 58.330 1.00 8.30 C
ANISOU 1240 CB LEU A 167 964 1020 1168 45 -30 -34 C
ATOM 1241 CG LEU A 167 31.227 44.223 57.677 1.00 8.82 C
ANISOU 1241 CG LEU A 167 1027 1084 1241 40 -29 -41 C
ATOM 1242 CD1 LEU A 167 30.854 42.822 58.142 1.00 8.82 C
ANISOU 1242 CD1 LEU A 167 1021 1080 1251 41 -27 -37 C
ATOM 1243 CD2 LEU A 167 31.173 44.353 56.162 1.00 9.34 C
ANISOU 1243 CD2 LEU A 167 1093 1151 1304 32 -32 -48 C
ATOM 1244 N LYS A 168 29.018 48.297 57.796 1.00 8.04 N
ANISOU 1244 N LYS A 168 944 991 1118 51 -32 -29 N
ATOM 1245 CA LYS A 168 27.965 49.241 58.111 1.00 8.86 C
ANISOU 1245 CA LYS A 168 1052 1097 1218 59 -30 -23 C
ATOM 1246 C LYS A 168 27.247 49.549 56.764 1.00 8.26 C
ANISOU 1246 C LYS A 168 973 1024 1140 56 -33 -22 C
ATOM 1247 O LYS A 168 27.737 49.195 55.692 1.00 7.84 O
ANISOU 1247 O LYS A 168 919 972 1089 48 -36 -27 O
ATOM 1248 CB LYS A 168 28.512 50.519 58.719 1.00 9.14 C
ANISOU 1248 CB LYS A 168 1099 1128 1245 63 -29 -25 C
ATOM 1249 CG LYS A 168 29.549 51.214 57.889 1.00 9.86 C
ANISOU 1249 CG LYS A 168 1198 1217 1333 56 -32 -31 C
ATOM 1250 CD LYS A 168 30.031 52.432 58.628 1.00 10.28 C
ANISOU 1250 CD LYS A 168 1264 1265 1379 58 -31 -33 C
ATOM 1251 CE LYS A 168 31.107 53.123 57.897 1.00 11.22 C
ANISOU 1251 CE LYS A 168 1389 1380 1494 49 -33 -38 C
ATOM 1252 NZ LYS A 168 31.399 54.388 58.601 1.00 11.66 N
ANISOU 1252 NZ LYS A 168 1458 1429 1543 51 -32 -40 N
ATOM 1253 N PRO A 169 26.062 50.167 56.813 1.00 8.33 N
ANISOU 1253 N PRO A 169 981 1035 1147 64 -32 -14 N
ATOM 1254 CA PRO A 169 25.296 50.293 55.565 1.00 8.48 C
ANISOU 1254 CA PRO A 169 995 1060 1166 62 -36 -11 C
ATOM 1255 C PRO A 169 26.009 51.028 54.423 1.00 8.54 C
ANISOU 1255 C PRO A 169 1010 1068 1168 56 -39 -16 C
ATOM 1256 O PRO A 169 25.897 50.612 53.279 1.00 8.85 O
ANISOU 1256 O PRO A 169 1044 1112 1207 48 -43 -18 O
ATOM 1257 CB PRO A 169 24.024 51.020 56.016 1.00 8.46 C
ANISOU 1257 CB PRO A 169 991 1061 1162 74 -33 -1 C
ATOM 1258 CG PRO A 169 23.853 50.521 57.418 1.00 8.91 C
ANISOU 1258 CG PRO A 169 1046 1117 1223 80 -28 1 C
ATOM 1259 CD PRO A 169 25.247 50.508 57.982 1.00 8.57 C
ANISOU 1259 CD PRO A 169 1013 1067 1178 76 -27 -7 C
ATOM 1260 N SER A 170 26.798 52.072 54.734 1.00 8.54 N
ANISOU 1260 N SER A 170 1022 1060 1163 58 -37 -18 N
ATOM 1261 CA SER A 170 27.495 52.829 53.723 1.00 8.82 C
ANISOU 1261 CA SER A 170 1065 1094 1193 52 -39 -20 C
ATOM 1262 C SER A 170 28.632 52.052 53.072 1.00 8.54 C
ANISOU 1262 C SER A 170 1027 1060 1158 40 -41 -29 C
ATOM 1263 O SER A 170 29.109 52.491 52.026 1.00 9.93 O
ANISOU 1263 O SER A 170 1206 1237 1329 34 -42 -30 O
ATOM 1264 CB SER A 170 27.913 54.169 54.275 1.00 9.56 C
ANISOU 1264 CB SER A 170 1172 1178 1281 57 -36 -19 C
ATOM 1265 OG SER A 170 28.823 53.992 55.327 1.00 10.37 O
ANISOU 1265 OG SER A 170 1278 1276 1385 55 -34 -25 O
ATOM 1266 N ASN A 171 29.024 50.910 53.648 1.00 8.04 N
ANISOU 1266 N ASN A 171 958 997 1101 38 -40 -34 N
ATOM 1267 CA ASN A 171 30.019 50.059 53.009 1.00 7.97 C
ANISOU 1267 CA ASN A 171 945 990 1094 28 -40 -42 C
ATOM 1268 C ASN A 171 29.432 48.869 52.283 1.00 8.24 C
ANISOU 1268 C ASN A 171 970 1028 1132 24 -42 -44 C
ATOM 1269 O ASN A 171 30.137 47.913 51.972 1.00 8.26 O
ANISOU 1269 O ASN A 171 970 1031 1138 18 -42 -51 O
ATOM 1270 CB ASN A 171 31.063 49.587 54.034 1.00 8.41 C
ANISOU 1270 CB ASN A 171 1001 1042 1153 28 -38 -46 C
ATOM 1271 CG ASN A 171 31.987 50.716 54.481 1.00 8.55 C
ANISOU 1271 CG ASN A 171 1028 1056 1166 27 -38 -47 C
ATOM 1272 OD1 ASN A 171 32.138 51.737 53.737 1.00 9.21 O
ANISOU 1272 OD1 ASN A 171 1118 1138 1243 24 -38 -46 O
ATOM 1273 ND2 ASN A 171 32.567 50.614 55.682 1.00 8.45 N
ANISOU 1273 ND2 ASN A 171 1016 1040 1154 30 -37 -48 N
ATOM 1274 N LEU A 172 28.143 48.920 51.976 1.00 7.93 N
ANISOU 1274 N LEU A 172 927 994 1093 27 -45 -38 N
ATOM 1275 CA LEU A 172 27.473 47.842 51.241 1.00 8.26 C
ANISOU 1275 CA LEU A 172 959 1040 1137 20 -48 -41 C
ATOM 1276 C LEU A 172 26.896 48.539 50.002 1.00 8.20 C
ANISOU 1276 C LEU A 172 952 1041 1121 18 -52 -38 C
ATOM 1277 O LEU A 172 25.891 49.261 50.045 1.00 8.21 O
ANISOU 1277 O LEU A 172 952 1046 1120 25 -54 -29 O
ATOM 1278 CB LEU A 172 26.360 47.250 52.120 1.00 7.92 C
ANISOU 1278 CB LEU A 172 909 999 1103 25 -47 -34 C
ATOM 1279 CG LEU A 172 26.878 46.638 53.410 1.00 7.79 C
ANISOU 1279 CG LEU A 172 892 974 1093 28 -42 -35 C
ATOM 1280 CD1 LEU A 172 25.699 46.148 54.182 1.00 8.23 C
ANISOU 1280 CD1 LEU A 172 941 1032 1155 32 -41 -27 C
ATOM 1281 CD2 LEU A 172 27.857 45.495 53.213 1.00 7.66 C
ANISOU 1281 CD2 LEU A 172 876 954 1082 21 -41 -44 C
ATOM 1282 N LEU A 173 27.491 48.234 48.860 1.00 7.53 N
ANISOU 1282 N LEU A 173 869 960 1032 10 -54 -46 N
ATOM 1283 CA LEU A 173 27.156 48.886 47.611 1.00 7.80 C
ANISOU 1283 CA LEU A 173 904 1002 1056 7 -58 -43 C
ATOM 1284 C LEU A 173 26.116 48.042 46.889 1.00 8.22 C
ANISOU 1284 C LEU A 173 949 1065 1110 1 -63 -45 C
ATOM 1285 O LEU A 173 26.154 46.773 46.941 1.00 8.56 O
ANISOU 1285 O LEU A 173 987 1106 1159 -5 -63 -53 O
ATOM 1286 CB LEU A 173 28.406 48.950 46.736 1.00 8.23 C
ANISOU 1286 CB LEU A 173 965 1057 1104 0 -56 -51 C
ATOM 1287 CG LEU A 173 29.606 49.651 47.330 1.00 8.42 C
ANISOU 1287 CG LEU A 173 996 1073 1128 2 -51 -52 C
ATOM 1288 CD1 LEU A 173 30.795 49.602 46.368 1.00 8.69 C
ANISOU 1288 CD1 LEU A 173 1034 1111 1156 -5 -48 -59 C
ATOM 1289 CD2 LEU A 173 29.327 51.043 47.787 1.00 8.88 C
ANISOU 1289 CD2 LEU A 173 1061 1128 1183 10 -50 -41 C
ATOM 1290 N ILE A 174 25.180 48.696 46.189 1.00 8.83 N
ANISOU 1290 N ILE A 174 1023 1152 1179 3 -69 -37 N
ATOM 1291 CA ILE A 174 24.021 47.987 45.594 1.00 9.80 C
ANISOU 1291 CA ILE A 174 1135 1286 1302 -3 -76 -37 C
ATOM 1292 C ILE A 174 23.800 48.502 44.177 1.00 11.36 C
ANISOU 1292 C ILE A 174 1333 1496 1486 -7 -82 -35 C
ATOM 1293 O ILE A 174 23.939 49.695 43.939 1.00 10.47 O
ANISOU 1293 O ILE A 174 1227 1386 1367 0 -81 -26 O
ATOM 1294 CB ILE A 174 22.741 48.143 46.467 1.00 10.97 C
ANISOU 1294 CB ILE A 174 1275 1438 1457 5 -77 -25 C
ATOM 1295 CG1 ILE A 174 22.966 47.657 47.893 1.00 11.08 C
ANISOU 1295 CG1 ILE A 174 1288 1439 1482 9 -70 -25 C
ATOM 1296 CG2 ILE A 174 21.560 47.488 45.819 1.00 11.37 C
ANISOU 1296 CG2 ILE A 174 1312 1500 1506 -2 -85 -24 C
ATOM 1297 CD1 ILE A 174 21.941 48.080 48.906 1.00 12.49 C
ANISOU 1297 CD1 ILE A 174 1461 1620 1666 20 -68 -13 C
ATOM 1298 N ASN A 175 23.501 47.606 43.253 1.00 13.39 N
ANISOU 1298 N ASN A 175 1586 1762 1739 -18 -87 -43 N
ATOM 1299 CA ASN A 175 23.225 47.999 41.844 1.00 16.01 C
ANISOU 1299 CA ASN A 175 1917 2109 2055 -23 -94 -42 C
ATOM 1300 C ASN A 175 21.775 47.858 41.509 1.00 17.88 C
ANISOU 1300 C ASN A 175 2142 2361 2291 -25 -104 -35 C
ATOM 1301 O ASN A 175 20.943 47.535 42.394 1.00 18.03 O
ANISOU 1301 O ASN A 175 2151 2378 2320 -22 -104 -30 O
ATOM 1302 CB ASN A 175 24.161 47.329 40.859 1.00 16.65 C
ANISOU 1302 CB ASN A 175 2005 2191 2129 -34 -94 -58 C
ATOM 1303 CG ASN A 175 23.882 45.854 40.707 1.00 17.50 C
ANISOU 1303 CG ASN A 175 2107 2299 2242 -46 -96 -71 C
ATOM 1304 OD1 ASN A 175 22.860 45.346 41.188 1.00 17.98 O
ANISOU 1304 OD1 ASN A 175 2159 2362 2312 -48 -101 -68 O
ATOM 1305 ND2 ASN A 175 24.794 45.146 40.059 1.00 20.16 N
ANISOU 1305 ND2 ASN A 175 2451 2633 2576 -53 -93 -86 N
ATOM 1306 N THR A 176 21.418 48.133 40.238 1.00 21.05 N
ANISOU 1306 N THR A 176 2542 2779 2678 -29 -112 -33 N
ATOM 1307 CA THR A 176 20.007 48.160 39.869 1.00 24.04 C
ANISOU 1307 CA THR A 176 2907 3175 3053 -30 -122 -24 C
ATOM 1308 C THR A 176 19.346 46.780 39.808 1.00 26.09 C
ANISOU 1308 C THR A 176 3156 3438 3317 -45 -128 -35 C
ATOM 1309 O THR A 176 18.117 46.690 39.838 1.00 26.87 O
ANISOU 1309 O THR A 176 3242 3551 3418 -46 -136 -26 O
ATOM 1310 CB THR A 176 19.805 48.843 38.508 1.00 26.08 C
ANISOU 1310 CB THR A 176 3166 3451 3292 -31 -130 -18 C
ATOM 1311 OG1 THR A 176 20.628 48.208 37.541 1.00 27.39 O
ANISOU 1311 OG1 THR A 176 3340 3619 3449 -44 -130 -35 O
ATOM 1312 CG2 THR A 176 20.156 50.351 38.610 1.00 27.86 C
ANISOU 1312 CG2 THR A 176 3400 3671 3513 -16 -124 -3 C
ATOM 1313 N THR A 177 20.140 45.714 39.766 1.00 23.00 N
ANISOU 1313 N THR A 177 2771 3036 2930 -56 -124 -52 N
ATOM 1314 CA THR A 177 19.583 44.369 39.885 1.00 25.71 C
ANISOU 1314 CA THR A 177 3107 3378 3282 -70 -128 -63 C
ATOM 1315 C THR A 177 19.650 43.802 41.339 1.00 21.94 C
ANISOU 1315 C THR A 177 2628 2884 2824 -66 -120 -62 C
ATOM 1316 O THR A 177 19.426 42.604 41.546 1.00 22.90 O
ANISOU 1316 O THR A 177 2747 2999 2955 -77 -121 -71 O
ATOM 1317 CB THR A 177 20.257 43.412 38.879 1.00 27.73 C
ANISOU 1317 CB THR A 177 3372 3634 3531 -84 -130 -83 C
ATOM 1318 OG1 THR A 177 21.657 43.624 38.872 1.00 31.23 O
ANISOU 1318 OG1 THR A 177 3828 4065 3972 -79 -120 -90 O
ATOM 1319 CG2 THR A 177 19.733 43.701 37.457 1.00 31.62 C
ANISOU 1319 CG2 THR A 177 3861 4149 4004 -92 -141 -84 C
ATOM 1320 N CYS A 178 19.871 44.682 42.325 1.00 19.39 N
ANISOU 1320 N CYS A 178 2307 2553 2507 -50 -113 -50 N
ATOM 1321 CA CYS A 178 19.901 44.346 43.767 1.00 20.43 C
ANISOU 1321 CA CYS A 178 2437 2670 2654 -44 -105 -46 C
ATOM 1322 C CYS A 178 21.098 43.461 44.138 1.00 15.98 C
ANISOU 1322 C CYS A 178 1884 2089 2098 -48 -97 -60 C
ATOM 1323 O CYS A 178 21.107 42.834 45.217 1.00 15.58 O
ANISOU 1323 O CYS A 178 1831 2027 2061 -47 -92 -59 O
ATOM 1324 CB CYS A 178 18.622 43.714 44.281 1.00 22.69 C
ANISOU 1324 CB CYS A 178 2708 2962 2950 -49 -109 -40 C
ATOM 1325 SG CYS A 178 17.229 44.874 44.231 1.00 31.52 S
ANISOU 1325 SG CYS A 178 3813 4101 4063 -38 -115 -19 S
ATOM 1326 N ASP A 179 22.117 43.440 43.293 1.00 14.10 N
ANISOU 1326 N ASP A 179 1656 1849 1852 -52 -96 -71 N
ATOM 1327 CA ASP A 179 23.389 42.816 43.648 1.00 13.35 C
ANISOU 1327 CA ASP A 179 1571 1739 1764 -52 -87 -83 C
ATOM 1328 C ASP A 179 24.078 43.707 44.684 1.00 11.70 C
ANISOU 1328 C ASP A 179 1366 1521 1557 -38 -80 -74 C
ATOM 1329 O ASP A 179 24.052 44.948 44.602 1.00 13.04 O
ANISOU 1329 O ASP A 179 1538 1697 1720 -30 -80 -64 O
ATOM 1330 CB ASP A 179 24.336 42.749 42.462 1.00 15.04 C
ANISOU 1330 CB ASP A 179 1794 1956 1966 -57 -87 -95 C
ATOM 1331 CG ASP A 179 23.813 41.926 41.327 1.00 17.75 C
ANISOU 1331 CG ASP A 179 2135 2308 2303 -71 -94 -107 C
ATOM 1332 OD1 ASP A 179 23.105 40.921 41.564 1.00 18.25 O
ANISOU 1332 OD1 ASP A 179 2193 2367 2375 -80 -97 -111 O
ATOM 1333 OD2 ASP A 179 24.234 42.254 40.183 1.00 22.10 O
ANISOU 1333 OD2 ASP A 179 2692 2868 2839 -75 -96 -113 O
ATOM 1334 N LEU A 180 24.629 43.079 45.689 1.00 9.82 N
ANISOU 1334 N LEU A 180 1130 1270 1332 -35 -73 -76 N
ATOM 1335 CA LEU A 180 25.289 43.760 46.807 1.00 9.08 C
ANISOU 1335 CA LEU A 180 1040 1168 1241 -23 -66 -69 C
ATOM 1336 C LEU A 180 26.764 43.381 46.893 1.00 8.65 C
ANISOU 1336 C LEU A 180 993 1104 1189 -23 -60 -79 C
ATOM 1337 O LEU A 180 27.121 42.235 46.725 1.00 9.29 O
ANISOU 1337 O LEU A 180 1075 1179 1276 -29 -58 -89 O
ATOM 1338 CB LEU A 180 24.567 43.401 48.091 1.00 8.93 C
ANISOU 1338 CB LEU A 180 1014 1144 1234 -19 -64 -61 C
ATOM 1339 CG LEU A 180 25.129 44.024 49.386 1.00 9.03 C
ANISOU 1339 CG LEU A 180 1031 1149 1250 -7 -58 -53 C
ATOM 1340 CD1 LEU A 180 23.969 44.215 50.366 1.00 9.65 C
ANISOU 1340 CD1 LEU A 180 1102 1230 1334 0 -58 -41 C
ATOM 1341 CD2 LEU A 180 26.201 43.139 50.031 1.00 9.60 C
ANISOU 1341 CD2 LEU A 180 1107 1209 1331 -7 -52 -60 C
ATOM 1342 N LYS A 181 27.615 44.400 47.067 1.00 8.05 N
ANISOU 1342 N LYS A 181 924 1028 1108 -16 -57 -75 N
ATOM 1343 CA LYS A 181 29.056 44.198 47.221 1.00 8.26 C
ANISOU 1343 CA LYS A 181 956 1048 1137 -15 -51 -82 C
ATOM 1344 C LYS A 181 29.578 44.950 48.439 1.00 7.84 C
ANISOU 1344 C LYS A 181 905 989 1086 -6 -47 -75 C
ATOM 1345 O LYS A 181 29.342 46.141 48.602 1.00 8.16 O
ANISOU 1345 O LYS A 181 947 1032 1120 -2 -48 -67 O
ATOM 1346 CB LYS A 181 29.784 44.671 45.995 1.00 8.86 C
ANISOU 1346 CB LYS A 181 1036 1130 1200 -19 -50 -88 C
ATOM 1347 CG LYS A 181 29.476 43.885 44.737 1.00 9.76 C
ANISOU 1347 CG LYS A 181 1149 1249 1309 -28 -53 -98 C
ATOM 1348 CD LYS A 181 30.183 44.470 43.532 1.00 10.88 C
ANISOU 1348 CD LYS A 181 1297 1400 1438 -32 -52 -103 C
ATOM 1349 CE LYS A 181 29.707 43.912 42.248 1.00 12.12 C
ANISOU 1349 CE LYS A 181 1453 1565 1585 -41 -57 -112 C
ATOM 1350 NZ LYS A 181 29.916 42.466 42.076 1.00 13.76 N
ANISOU 1350 NZ LYS A 181 1662 1767 1800 -46 -54 -126 N
ATOM 1351 N ILE A 182 30.348 44.245 49.227 1.00 7.82 N
ANISOU 1351 N ILE A 182 901 978 1091 -4 -43 -78 N
ATOM 1352 CA ILE A 182 31.027 44.796 50.372 1.00 7.37 C
ANISOU 1352 CA ILE A 182 846 917 1036 3 -40 -73 C
ATOM 1353 C ILE A 182 32.256 45.578 49.964 1.00 7.41 C
ANISOU 1353 C ILE A 182 856 925 1034 2 -38 -76 C
ATOM 1354 O ILE A 182 33.046 45.116 49.168 1.00 6.76 O
ANISOU 1354 O ILE A 182 774 844 951 -2 -35 -84 O
ATOM 1355 CB ILE A 182 31.435 43.700 51.365 1.00 7.52 C
ANISOU 1355 CB ILE A 182 862 928 1066 7 -36 -74 C
ATOM 1356 CG1 ILE A 182 30.227 42.950 51.929 1.00 7.79 C
ANISOU 1356 CG1 ILE A 182 892 960 1109 7 -37 -69 C
ATOM 1357 CG2 ILE A 182 32.284 44.297 52.509 1.00 7.87 C
ANISOU 1357 CG2 ILE A 182 909 971 1110 13 -34 -69 C
ATOM 1358 CD1 ILE A 182 30.593 41.621 52.488 1.00 7.77 C
ANISOU 1358 CD1 ILE A 182 887 949 1117 8 -33 -71 C
ATOM 1359 N CYS A 183 32.417 46.763 50.525 1.00 7.18 N
ANISOU 1359 N CYS A 183 832 896 1001 6 -38 -69 N
ATOM 1360 CA CYS A 183 33.601 47.620 50.234 1.00 7.89 C
ANISOU 1360 CA CYS A 183 926 987 1084 3 -36 -71 C
ATOM 1361 C CYS A 183 34.273 48.082 51.547 1.00 7.86 C
ANISOU 1361 C CYS A 183 924 979 1083 7 -35 -68 C
ATOM 1362 O CYS A 183 33.744 47.904 52.654 1.00 8.31 O
ANISOU 1362 O CYS A 183 980 1033 1145 13 -36 -63 O
ATOM 1363 CB CYS A 183 33.253 48.807 49.330 1.00 8.06 C
ANISOU 1363 CB CYS A 183 953 1012 1096 0 -38 -67 C
ATOM 1364 SG CYS A 183 32.306 50.140 50.104 1.00 8.99 S
ANISOU 1364 SG CYS A 183 1078 1127 1212 7 -41 -56 S
ATOM 1365 N ASP A 184 35.446 48.720 51.370 1.00 7.93 N
ANISOU 1365 N ASP A 184 935 990 1088 3 -34 -70 N
ATOM 1366 CA ASP A 184 36.243 49.415 52.407 1.00 8.12 C
ANISOU 1366 CA ASP A 184 962 1012 1111 3 -34 -68 C
ATOM 1367 C ASP A 184 36.923 48.437 53.376 1.00 7.83 C
ANISOU 1367 C ASP A 184 918 975 1081 7 -33 -69 C
ATOM 1368 O ASP A 184 36.393 48.104 54.469 1.00 8.44 O
ANISOU 1368 O ASP A 184 996 1050 1163 13 -34 -66 O
ATOM 1369 CB ASP A 184 35.483 50.460 53.211 1.00 8.92 C
ANISOU 1369 CB ASP A 184 1071 1108 1209 7 -36 -62 C
ATOM 1370 CG ASP A 184 36.448 51.455 53.879 1.00 9.80 C
ANISOU 1370 CG ASP A 184 1188 1218 1317 3 -37 -62 C
ATOM 1371 OD1 ASP A 184 37.659 51.068 54.006 1.00 8.98 O
ANISOU 1371 OD1 ASP A 184 1079 1119 1215 -1 -36 -66 O
ATOM 1372 OD2 ASP A 184 36.006 52.596 54.290 1.00 11.30 O
ANISOU 1372 OD2 ASP A 184 1388 1402 1503 5 -38 -58 O
ATOM 1373 N PHE A 185 38.104 47.998 52.995 1.00 7.90 N
ANISOU 1373 N PHE A 185 922 988 1091 3 -31 -74 N
ATOM 1374 CA PHE A 185 38.910 47.093 53.784 1.00 8.05 C
ANISOU 1374 CA PHE A 185 934 1009 1117 8 -30 -75 C
ATOM 1375 C PHE A 185 40.083 47.823 54.460 1.00 8.14 C
ANISOU 1375 C PHE A 185 944 1025 1124 4 -31 -74 C
ATOM 1376 O PHE A 185 41.078 47.189 54.878 1.00 7.88 O
ANISOU 1376 O PHE A 185 902 996 1095 6 -30 -74 O
ATOM 1377 CB PHE A 185 39.399 45.945 52.904 1.00 8.18 C
ANISOU 1377 CB PHE A 185 944 1027 1138 8 -25 -81 C
ATOM 1378 CG PHE A 185 38.305 44.952 52.570 1.00 8.16 C
ANISOU 1378 CG PHE A 185 942 1019 1141 11 -24 -82 C
ATOM 1379 CD1 PHE A 185 37.336 45.268 51.648 1.00 8.22 C
ANISOU 1379 CD1 PHE A 185 953 1026 1143 7 -25 -84 C
ATOM 1380 CD2 PHE A 185 38.168 43.765 53.289 1.00 8.61 C
ANISOU 1380 CD2 PHE A 185 995 1071 1207 18 -23 -81 C
ATOM 1381 CE1 PHE A 185 36.296 44.400 51.335 1.00 8.10 C
ANISOU 1381 CE1 PHE A 185 938 1007 1133 8 -26 -85 C
ATOM 1382 CE2 PHE A 185 37.141 42.895 52.973 1.00 8.32 C
ANISOU 1382 CE2 PHE A 185 958 1027 1174 19 -22 -83 C
ATOM 1383 CZ PHE A 185 36.225 43.222 51.978 1.00 7.99 C
ANISOU 1383 CZ PHE A 185 921 987 1129 13 -24 -86 C
ATOM 1384 N GLY A 186 39.969 49.144 54.667 1.00 8.17 N
ANISOU 1384 N GLY A 186 955 1027 1121 -1 -34 -72 N
ATOM 1385 CA GLY A 186 41.067 49.906 55.262 1.00 8.48 C
ANISOU 1385 CA GLY A 186 994 1070 1157 -7 -37 -72 C
ATOM 1386 C GLY A 186 41.394 49.500 56.688 1.00 8.87 C
ANISOU 1386 C GLY A 186 1039 1122 1208 -2 -40 -70 C
ATOM 1387 O GLY A 186 42.538 49.717 57.113 1.00 9.44 O
ANISOU 1387 O GLY A 186 1106 1201 1278 -7 -42 -70 O
ATOM 1388 N LEU A 187 40.430 49.000 57.429 1.00 8.58 N
ANISOU 1388 N LEU A 187 1005 1080 1173 7 -40 -67 N
ATOM 1389 CA LEU A 187 40.647 48.575 58.827 1.00 9.23 C
ANISOU 1389 CA LEU A 187 1085 1166 1257 13 -43 -64 C
ATOM 1390 C LEU A 187 40.725 47.096 58.939 1.00 8.73 C
ANISOU 1390 C LEU A 187 1012 1104 1202 21 -40 -61 C
ATOM 1391 O LEU A 187 40.735 46.530 60.043 1.00 9.58 O
ANISOU 1391 O LEU A 187 1117 1213 1311 29 -41 -57 O
ATOM 1392 CB LEU A 187 39.586 49.104 59.793 1.00 10.07 C
ANISOU 1392 CB LEU A 187 1201 1267 1359 18 -44 -61 C
ATOM 1393 CG LEU A 187 39.597 50.648 59.883 1.00 10.85 C
ANISOU 1393 CG LEU A 187 1311 1363 1449 11 -47 -63 C
ATOM 1394 CD1 LEU A 187 38.438 51.080 60.772 1.00 11.75 C
ANISOU 1394 CD1 LEU A 187 1435 1471 1559 18 -47 -61 C
ATOM 1395 CD2 LEU A 187 40.889 51.177 60.399 1.00 12.54 C
ANISOU 1395 CD2 LEU A 187 1523 1583 1658 2 -51 -66 C
ATOM 1396 N ALA A 188 40.803 46.382 57.824 1.00 8.44 N
ANISOU 1396 N ALA A 188 970 1066 1171 21 -36 -64 N
ATOM 1397 CA ALA A 188 40.799 44.955 57.877 1.00 9.08 C
ANISOU 1397 CA ALA A 188 1044 1144 1260 29 -32 -63 C
ATOM 1398 C ALA A 188 42.078 44.392 58.500 1.00 9.50 C
ANISOU 1398 C ALA A 188 1087 1205 1316 34 -33 -61 C
ATOM 1399 O ALA A 188 43.141 45.022 58.393 1.00 10.11 O
ANISOU 1399 O ALA A 188 1161 1292 1390 28 -35 -62 O
ATOM 1400 CB ALA A 188 40.644 44.410 56.515 1.00 9.02 C
ANISOU 1400 CB ALA A 188 1035 1134 1257 27 -28 -69 C
ATOM 1401 N ARG A 189 41.953 43.224 59.154 1.00 9.32 N
ANISOU 1401 N ARG A 189 1060 1179 1301 44 -31 -55 N
ATOM 1402 CA AARG A 189 43.082 42.542 59.766 0.60 10.02 C
ANISOU 1402 CA AARG A 189 1139 1276 1393 50 -31 -51 C
ATOM 1403 CA BARG A 189 43.073 42.554 59.800 0.40 10.08 C
ANISOU 1403 CA BARG A 189 1147 1283 1401 50 -31 -51 C
ATOM 1404 C ARG A 189 42.883 41.059 59.662 1.00 9.62 C
ANISOU 1404 C ARG A 189 1085 1216 1354 61 -25 -49 C
ATOM 1405 O ARG A 189 41.880 40.610 59.137 1.00 10.19 O
ANISOU 1405 O ARG A 189 1163 1278 1431 60 -22 -51 O
ATOM 1406 CB AARG A 189 43.224 42.940 61.205 0.60 11.37 C
ANISOU 1406 CB AARG A 189 1310 1453 1558 53 -37 -44 C
ATOM 1407 CB BARG A 189 43.155 42.945 61.269 0.40 11.34 C
ANISOU 1407 CB BARG A 189 1306 1449 1554 53 -37 -44 C
ATOM 1408 CG AARG A 189 43.749 44.336 61.387 0.60 12.68 C
ANISOU 1408 CG AARG A 189 1478 1627 1713 42 -43 -48 C
ATOM 1409 CG BARG A 189 43.417 44.422 61.486 0.40 12.47 C
ANISOU 1409 CG BARG A 189 1454 1598 1685 42 -43 -47 C
ATOM 1410 CD AARG A 189 44.055 44.616 62.833 0.60 13.60 C
ANISOU 1410 CD AARG A 189 1594 1752 1822 44 -50 -42 C
ATOM 1411 CD BARG A 189 43.751 44.782 62.923 0.40 13.35 C
ANISOU 1411 CD BARG A 189 1566 1719 1790 44 -50 -42 C
ATOM 1412 NE AARG A 189 44.409 46.001 63.092 0.60 13.66 N
ANISOU 1412 NE AARG A 189 1606 1765 1819 33 -56 -47 N
ATOM 1413 NE BARG A 189 44.993 44.172 63.446 0.40 14.32 N
ANISOU 1413 NE BARG A 189 1675 1853 1913 48 -53 -38 N
ATOM 1414 CZ AARG A 189 45.625 46.517 63.001 0.60 14.87 C
ANISOU 1414 CZ AARG A 189 1752 1929 1968 24 -60 -49 C
ATOM 1415 CZ BARG A 189 46.175 44.786 63.489 0.40 14.40 C
ANISOU 1415 CZ BARG A 189 1677 1875 1918 41 -58 -40 C
ATOM 1416 NH1AARG A 189 45.795 47.820 63.308 0.60 15.97 N
ANISOU 1416 NH1AARG A 189 1899 2072 2098 12 -66 -54 N
ATOM 1417 NH1BARG A 189 47.239 44.183 64.021 0.40 14.93 N
ANISOU 1417 NH1BARG A 189 1731 1955 1986 47 -60 -34 N
ATOM 1418 NH2AARG A 189 46.674 45.756 62.642 0.60 15.20 N
ANISOU 1418 NH2AARG A 189 1779 1979 2016 28 -58 -47 N
ATOM 1419 NH2BARG A 189 46.305 46.009 62.998 0.40 15.24 N
ANISOU 1419 NH2BARG A 189 1789 1983 2018 27 -60 -47 N
ATOM 1420 N ILE A 190 43.843 40.280 60.126 1.00 9.61 N
ANISOU 1420 N ILE A 190 1075 1220 1358 69 -24 -44 N
ATOM 1421 CA ILE A 190 43.717 38.846 60.193 1.00 9.64 C
ANISOU 1421 CA ILE A 190 1075 1213 1372 80 -18 -40 C
ATOM 1422 C ILE A 190 43.269 38.407 61.574 1.00 10.09 C
ANISOU 1422 C ILE A 190 1133 1269 1431 88 -21 -28 C
ATOM 1423 O ILE A 190 43.695 38.983 62.609 1.00 9.62 O
ANISOU 1423 O ILE A 190 1072 1222 1364 89 -27 -22 O
ATOM 1424 CB ILE A 190 45.060 38.164 59.844 1.00 9.84 C
ANISOU 1424 CB ILE A 190 1090 1245 1404 88 -14 -40 C
ATOM 1425 CG1 ILE A 190 45.588 38.665 58.479 1.00 10.51 C
ANISOU 1425 CG1 ILE A 190 1173 1334 1485 81 -11 -51 C
ATOM 1426 CG2 ILE A 190 44.977 36.651 59.907 1.00 10.35 C
ANISOU 1426 CG2 ILE A 190 1154 1297 1482 101 -7 -36 C
ATOM 1427 CD1 ILE A 190 44.628 38.503 57.308 1.00 10.32 C
ANISOU 1427 CD1 ILE A 190 1159 1298 1464 75 -6 -61 C
ATOM 1428 N ALA A 191 42.462 37.347 61.619 1.00 9.82 N
ANISOU 1428 N ALA A 191 1103 1221 1406 94 -16 -25 N
ATOM 1429 CA ALA A 191 42.027 36.758 62.882 1.00 10.11 C
ANISOU 1429 CA ALA A 191 1140 1255 1445 102 -16 -12 C
ATOM 1430 C ALA A 191 43.261 36.426 63.700 1.00 10.41 C
ANISOU 1430 C ALA A 191 1168 1303 1483 112 -18 -3 C
ATOM 1431 O ALA A 191 44.207 35.838 63.207 1.00 11.02 O
ANISOU 1431 O ALA A 191 1239 1382 1567 118 -15 -5 O
ATOM 1432 CB ALA A 191 41.176 35.525 62.651 1.00 10.27 C
ANISOU 1432 CB ALA A 191 1166 1258 1480 106 -9 -10 C
ATOM 1433 N ASP A 192 43.266 36.867 64.961 1.00 10.71 N
ANISOU 1433 N ASP A 192 1205 1352 1512 114 -24 6 N
ATOM 1434 CA ASP A 192 44.470 36.722 65.817 1.00 12.06 C
ANISOU 1434 CA ASP A 192 1366 1538 1679 123 -29 15 C
ATOM 1435 C ASP A 192 43.949 36.583 67.269 1.00 11.70 C
ANISOU 1435 C ASP A 192 1323 1495 1627 129 -32 28 C
ATOM 1436 O ASP A 192 44.187 37.489 68.107 1.00 11.30 O
ANISOU 1436 O ASP A 192 1272 1460 1563 125 -40 29 O
ATOM 1437 CB ASP A 192 45.350 37.942 65.658 1.00 13.76 C
ANISOU 1437 CB ASP A 192 1576 1769 1882 113 -36 7 C
ATOM 1438 CG ASP A 192 46.752 37.733 66.169 1.00 16.31 C
ANISOU 1438 CG ASP A 192 1886 2109 2204 121 -40 14 C
ATOM 1439 OD1 ASP A 192 47.050 36.643 66.700 1.00 17.59 O
ANISOU 1439 OD1 ASP A 192 2042 2270 2373 135 -38 26 O
ATOM 1440 OD2 ASP A 192 47.545 38.715 66.019 1.00 17.94 O
ANISOU 1440 OD2 ASP A 192 2086 2329 2401 111 -46 9 O
ATOM 1441 N PRO A 193 43.318 35.436 67.550 1.00 12.93 N
ANISOU 1441 N PRO A 193 1482 1638 1794 137 -26 37 N
ATOM 1442 CA PRO A 193 42.751 35.220 68.905 1.00 13.04 C
ANISOU 1442 CA PRO A 193 1498 1654 1802 143 -27 51 C
ATOM 1443 C PRO A 193 43.825 35.320 69.995 1.00 13.64 C
ANISOU 1443 C PRO A 193 1565 1749 1868 151 -35 61 C
ATOM 1444 O PRO A 193 43.525 35.793 71.101 1.00 12.56 O
ANISOU 1444 O PRO A 193 1432 1624 1719 151 -40 68 O
ATOM 1445 CB PRO A 193 42.180 33.783 68.813 1.00 13.82 C
ANISOU 1445 CB PRO A 193 1599 1734 1917 152 -18 60 C
ATOM 1446 CG PRO A 193 42.876 33.146 67.660 1.00 15.29 C
ANISOU 1446 CG PRO A 193 1782 1912 2117 154 -13 53 C
ATOM 1447 CD PRO A 193 43.050 34.275 66.675 1.00 14.26 C
ANISOU 1447 CD PRO A 193 1652 1787 1979 142 -16 36 C
ATOM 1448 N GLU A 194 45.071 34.962 69.692 1.00 12.08 N
ANISOU 1448 N GLU A 194 1356 1558 1674 157 -36 62 N
ATOM 1449 CA AGLU A 194 46.119 35.052 70.705 0.50 12.72 C
ANISOU 1449 CA AGLU A 194 1427 1660 1746 165 -44 73 C
ATOM 1450 CA BGLU A 194 46.134 35.082 70.680 0.50 12.90 C
ANISOU 1450 CA BGLU A 194 1450 1683 1768 164 -44 72 C
ATOM 1451 C GLU A 194 46.228 36.462 71.263 1.00 12.65 C
ANISOU 1451 C GLU A 194 1421 1669 1718 152 -54 66 C
ATOM 1452 O GLU A 194 46.504 36.620 72.486 1.00 13.84 O
ANISOU 1452 O GLU A 194 1568 1835 1856 156 -62 76 O
ATOM 1453 CB AGLU A 194 47.517 34.587 70.183 0.50 12.41 C
ANISOU 1453 CB AGLU A 194 1374 1628 1714 172 -44 74 C
ATOM 1454 CB BGLU A 194 47.495 34.789 70.061 0.50 12.86 C
ANISOU 1454 CB BGLU A 194 1431 1686 1770 170 -44 71 C
ATOM 1455 CG AGLU A 194 48.699 35.053 71.066 0.50 12.94 C
ANISOU 1455 CG AGLU A 194 1427 1722 1768 175 -55 81 C
ATOM 1456 CG BGLU A 194 47.739 33.362 69.776 0.50 13.49 C
ANISOU 1456 CG BGLU A 194 1507 1752 1866 186 -35 80 C
ATOM 1457 CD AGLU A 194 50.024 34.507 70.657 0.50 12.80 C
ANISOU 1457 CD AGLU A 194 1393 1712 1757 185 -54 85 C
ATOM 1458 CD BGLU A 194 48.952 33.174 68.941 0.50 13.71 C
ANISOU 1458 CD BGLU A 194 1522 1785 1900 190 -33 76 C
ATOM 1459 OE1AGLU A 194 50.155 34.097 69.498 0.50 13.39 O
ANISOU 1459 OE1AGLU A 194 1467 1775 1845 186 -45 77 O
ATOM 1460 OE1BGLU A 194 50.077 33.373 69.460 0.50 14.36 O
ANISOU 1460 OE1BGLU A 194 1590 1889 1976 195 -40 82 O
ATOM 1461 OE2AGLU A 194 50.940 34.530 71.493 0.50 11.87 O
ANISOU 1461 OE2AGLU A 194 1263 1616 1632 191 -62 95 O
ATOM 1462 OE2BGLU A 194 48.735 32.767 67.798 0.50 13.11 O
ANISOU 1462 OE2BGLU A 194 1451 1694 1837 190 -24 66 O
ATOM 1463 N HIS A 195 45.999 37.479 70.417 1.00 12.14 N
ANISOU 1463 N HIS A 195 1362 1602 1651 138 -55 50 N
ATOM 1464 CA HIS A 195 46.238 38.873 70.776 1.00 13.50 C
ANISOU 1464 CA HIS A 195 1535 1788 1806 125 -65 42 C
ATOM 1465 C HIS A 195 44.979 39.738 70.900 1.00 12.89 C
ANISOU 1465 C HIS A 195 1473 1703 1721 116 -64 34 C
ATOM 1466 O HIS A 195 45.076 40.988 70.850 1.00 12.94 O
ANISOU 1466 O HIS A 195 1485 1715 1716 104 -70 23 O
ATOM 1467 CB HIS A 195 47.185 39.467 69.751 1.00 14.58 C
ANISOU 1467 CB HIS A 195 1666 1931 1945 116 -67 30 C
ATOM 1468 CG HIS A 195 48.537 38.834 69.778 1.00 15.90 C
ANISOU 1468 CG HIS A 195 1815 2110 2116 124 -69 38 C
ATOM 1469 ND1 HIS A 195 49.050 38.094 68.738 1.00 17.25 N
ANISOU 1469 ND1 HIS A 195 1978 2275 2301 130 -61 36 N
ATOM 1470 CD2 HIS A 195 49.425 38.712 70.798 1.00 19.04 C
ANISOU 1470 CD2 HIS A 195 2202 2528 2506 130 -77 48 C
ATOM 1471 CE1 HIS A 195 50.259 37.665 69.071 1.00 17.11 C
ANISOU 1471 CE1 HIS A 195 1944 2272 2283 139 -65 45 C
ATOM 1472 NE2 HIS A 195 50.500 38.018 70.314 1.00 19.46 N
ANISOU 1472 NE2 HIS A 195 2239 2587 2568 139 -75 53 N
ATOM 1473 N ASP A 196 43.835 39.080 71.083 1.00 12.33 N
ANISOU 1473 N ASP A 196 1410 1619 1656 123 -57 40 N
ATOM 1474 CA ASP A 196 42.548 39.818 71.120 1.00 12.01 C
ANISOU 1474 CA ASP A 196 1383 1571 1610 116 -54 34 C
ATOM 1475 C ASP A 196 42.397 40.698 72.358 1.00 12.19 C
ANISOU 1475 C ASP A 196 1411 1606 1614 114 -61 35 C
ATOM 1476 O ASP A 196 41.654 41.688 72.341 1.00 12.07 O
ANISOU 1476 O ASP A 196 1407 1588 1591 107 -61 27 O
ATOM 1477 CB ASP A 196 41.374 38.881 71.021 1.00 12.04 C
ANISOU 1477 CB ASP A 196 1390 1559 1625 122 -45 42 C
ATOM 1478 CG ASP A 196 40.067 39.612 70.765 1.00 13.14 C
ANISOU 1478 CG ASP A 196 1541 1690 1762 115 -42 35 C
ATOM 1479 OD1 ASP A 196 39.920 40.208 69.672 1.00 14.41 O
ANISOU 1479 OD1 ASP A 196 1705 1846 1926 106 -41 23 O
ATOM 1480 OD2 ASP A 196 39.173 39.565 71.617 1.00 12.80 O
ANISOU 1480 OD2 ASP A 196 1503 1647 1714 119 -39 42 O
ATOM 1481 N HIS A 197 43.033 40.302 73.462 1.00 13.16 N
ANISOU 1481 N HIS A 197 1529 1743 1730 122 -66 46 N
ATOM 1482 CA HIS A 197 42.733 40.963 74.766 1.00 12.36 C
ANISOU 1482 CA HIS A 197 1434 1654 1609 122 -71 48 C
ATOM 1483 C HIS A 197 43.265 42.379 74.869 1.00 11.83 C
ANISOU 1483 C HIS A 197 1372 1597 1527 109 -80 34 C
ATOM 1484 O HIS A 197 44.379 42.679 74.421 1.00 13.20 O
ANISOU 1484 O HIS A 197 1537 1778 1701 102 -87 29 O
ATOM 1485 CB HIS A 197 43.309 40.177 75.909 1.00 13.05 C
ANISOU 1485 CB HIS A 197 1514 1755 1690 133 -75 64 C
ATOM 1486 CG HIS A 197 42.863 40.709 77.234 1.00 13.63 C
ANISOU 1486 CG HIS A 197 1596 1840 1743 134 -78 67 C
ATOM 1487 ND1 HIS A 197 43.640 41.513 78.013 1.00 14.26 N
ANISOU 1487 ND1 HIS A 197 1675 1938 1804 129 -90 62 N
ATOM 1488 CD2 HIS A 197 41.659 40.620 77.840 1.00 13.66 C
ANISOU 1488 CD2 HIS A 197 1609 1839 1743 139 -71 73 C
ATOM 1489 CE1 HIS A 197 42.923 41.902 79.072 1.00 14.76 C
ANISOU 1489 CE1 HIS A 197 1750 2008 1852 131 -89 64 C
ATOM 1490 NE2 HIS A 197 41.732 41.358 78.981 1.00 14.08 N
ANISOU 1490 NE2 HIS A 197 1669 1908 1774 138 -78 71 N
ATOM 1491 N THR A 198 42.479 43.270 75.467 1.00 11.08 N
ANISOU 1491 N THR A 198 1290 1502 1418 106 -80 29 N
ATOM 1492 CA THR A 198 42.942 44.582 75.783 1.00 10.69 C
ANISOU 1492 CA THR A 198 1247 1461 1353 94 -89 16 C
ATOM 1493 C THR A 198 42.165 45.092 77.010 1.00 10.94 C
ANISOU 1493 C THR A 198 1291 1497 1367 97 -88 16 C
ATOM 1494 O THR A 198 41.282 44.436 77.509 1.00 10.67 O
ANISOU 1494 O THR A 198 1259 1460 1333 108 -81 27 O
ATOM 1495 CB THR A 198 42.770 45.536 74.559 1.00 11.44 C
ANISOU 1495 CB THR A 198 1349 1544 1455 82 -87 1 C
ATOM 1496 OG1 THR A 198 43.399 46.776 74.825 1.00 12.49 O
ANISOU 1496 OG1 THR A 198 1488 1684 1575 69 -95 -11 O
ATOM 1497 CG2 THR A 198 41.301 45.781 74.274 1.00 11.89 C
ANISOU 1497 CG2 THR A 198 1417 1584 1515 85 -77 -1 C
ATOM 1498 N GLY A 199 42.498 46.259 77.509 1.00 10.54 N
ANISOU 1498 N GLY A 199 1250 1455 1300 88 -96 4 N
ATOM 1499 CA GLY A 199 41.853 46.829 78.673 1.00 11.26 C
ANISOU 1499 CA GLY A 199 1355 1552 1372 91 -96 2 C
ATOM 1500 C GLY A 199 40.492 47.437 78.397 1.00 12.15 C
ANISOU 1500 C GLY A 199 1483 1649 1487 93 -85 -4 C
ATOM 1501 O GLY A 199 40.087 47.620 77.266 1.00 13.55 O
ANISOU 1501 O GLY A 199 1660 1811 1678 90 -80 -9 O
ATOM 1502 N PHE A 200 39.837 47.872 79.466 1.00 11.92 N
ANISOU 1502 N PHE A 200 1464 1624 1440 98 -83 -5 N
ATOM 1503 CA PHE A 200 38.569 48.551 79.426 1.00 12.21 C
ANISOU 1503 CA PHE A 200 1516 1649 1475 102 -73 -11 C
ATOM 1504 C PHE A 200 38.750 49.914 78.782 1.00 12.97 C
ANISOU 1504 C PHE A 200 1624 1736 1570 89 -76 -29 C
ATOM 1505 O PHE A 200 39.703 50.631 79.071 1.00 13.41 O
ANISOU 1505 O PHE A 200 1684 1798 1614 78 -86 -40 O
ATOM 1506 CB PHE A 200 38.103 48.666 80.869 1.00 11.65 C
ANISOU 1506 CB PHE A 200 1454 1590 1383 111 -71 -8 C
ATOM 1507 CG PHE A 200 36.790 49.381 81.095 1.00 12.00 C
ANISOU 1507 CG PHE A 200 1513 1625 1421 117 -60 -13 C
ATOM 1508 CD1 PHE A 200 35.624 48.968 80.482 1.00 11.88 C
ANISOU 1508 CD1 PHE A 200 1495 1598 1421 125 -48 -6 C
ATOM 1509 CD2 PHE A 200 36.729 50.391 82.044 1.00 12.06 C
ANISOU 1509 CD2 PHE A 200 1537 1638 1406 117 -62 -25 C
ATOM 1510 CE1 PHE A 200 34.436 49.588 80.752 1.00 11.94 C
ANISOU 1510 CE1 PHE A 200 1515 1601 1423 133 -38 -9 C
ATOM 1511 CE2 PHE A 200 35.520 50.983 82.333 1.00 12.32 C
ANISOU 1511 CE2 PHE A 200 1583 1665 1433 125 -50 -29 C
ATOM 1512 CZ PHE A 200 34.398 50.581 81.681 1.00 12.04 C
ANISOU 1512 CZ PHE A 200 1543 1618 1414 134 -39 -20 C
ATOM 1513 N LEU A 201 37.749 50.261 77.971 1.00 13.41 N
ANISOU 1513 N LEU A 201 1685 1774 1636 92 -67 -32 N
ATOM 1514 CA LEU A 201 37.699 51.558 77.264 1.00 15.66 C
ANISOU 1514 CA LEU A 201 1983 2047 1921 82 -67 -47 C
ATOM 1515 C LEU A 201 38.954 51.840 76.413 1.00 16.28 C
ANISOU 1515 C LEU A 201 2055 2124 2006 67 -77 -54 C
ATOM 1516 O LEU A 201 39.458 52.960 76.395 1.00 19.54 O
ANISOU 1516 O LEU A 201 2479 2534 2411 55 -82 -68 O
ATOM 1517 CB LEU A 201 37.465 52.735 78.244 1.00 18.52 C
ANISOU 1517 CB LEU A 201 2365 2410 2263 82 -67 -60 C
ATOM 1518 CG LEU A 201 36.257 52.591 79.192 1.00 19.81 C
ANISOU 1518 CG LEU A 201 2535 2575 2416 98 -57 -54 C
ATOM 1519 CD1 LEU A 201 36.172 53.793 80.125 1.00 23.53 C
ANISOU 1519 CD1 LEU A 201 3027 3047 2866 97 -58 -68 C
ATOM 1520 CD2 LEU A 201 34.971 52.376 78.455 1.00 19.93 C
ANISOU 1520 CD2 LEU A 201 2548 2578 2445 108 -45 -47 C
ATOM 1521 N THR A 202 39.419 50.846 75.674 1.00 15.05 N
ANISOU 1521 N THR A 202 1882 1970 1865 66 -78 -46 N
ATOM 1522 CA THR A 202 40.517 51.003 74.694 1.00 15.21 C
ANISOU 1522 CA THR A 202 1895 1990 1895 53 -84 -51 C
ATOM 1523 C THR A 202 39.990 51.717 73.465 1.00 15.73 C
ANISOU 1523 C THR A 202 1968 2039 1971 48 -79 -57 C
ATOM 1524 O THR A 202 38.942 51.341 72.920 1.00 15.01 O
ANISOU 1524 O THR A 202 1876 1938 1889 57 -70 -52 O
ATOM 1525 CB THR A 202 41.097 49.627 74.263 1.00 14.75 C
ANISOU 1525 CB THR A 202 1817 1938 1849 57 -85 -39 C
ATOM 1526 OG1 THR A 202 41.685 48.944 75.424 1.00 16.18 O
ANISOU 1526 OG1 THR A 202 1990 2136 2021 63 -91 -30 O
ATOM 1527 CG2 THR A 202 42.221 49.787 73.210 1.00 15.68 C
ANISOU 1527 CG2 THR A 202 1926 2057 1977 45 -90 -44 C
ATOM 1528 N GLU A 203 40.715 52.740 73.018 1.00 15.97 N
ANISOU 1528 N GLU A 203 2004 2066 1999 34 -84 -68 N
ATOM 1529 CA GLU A 203 40.298 53.500 71.835 1.00 17.30 C
ANISOU 1529 CA GLU A 203 2180 2218 2176 28 -79 -74 C
ATOM 1530 C GLU A 203 40.199 52.564 70.624 1.00 16.29 C
ANISOU 1530 C GLU A 203 2038 2087 2065 31 -75 -66 C
ATOM 1531 O GLU A 203 40.946 51.596 70.485 1.00 16.13 O
ANISOU 1531 O GLU A 203 2002 2076 2050 31 -78 -60 O
ATOM 1532 CB GLU A 203 41.272 54.659 71.593 1.00 21.76 C
ANISOU 1532 CB GLU A 203 2752 2781 2735 10 -86 -86 C
ATOM 1533 CG GLU A 203 41.419 55.499 72.840 1.00 28.35 C
ANISOU 1533 CG GLU A 203 3601 3619 3553 6 -92 -95 C
ATOM 1534 CD GLU A 203 41.501 56.981 72.587 1.00 36.32 C
ANISOU 1534 CD GLU A 203 4628 4614 4556 -6 -92 -108 C
ATOM 1535 OE1 GLU A 203 42.504 57.397 71.936 1.00 44.33 O
ANISOU 1535 OE1 GLU A 203 5639 5629 5575 -23 -98 -112 O
ATOM 1536 OE2 GLU A 203 40.607 57.726 73.104 1.00 40.56 O
ANISOU 1536 OE2 GLU A 203 5184 5141 5086 0 -87 -113 O
ATOM 1537 N TYR A 204 39.246 52.845 69.745 1.00 16.41 N
ANISOU 1537 N TYR A 204 2059 2089 2087 34 -67 -66 N
ATOM 1538 CA TYR A 204 38.962 51.959 68.618 1.00 16.26 C
ANISOU 1538 CA TYR A 204 2028 2067 2083 38 -63 -60 C
ATOM 1539 C TYR A 204 38.656 52.806 67.422 1.00 17.92 C
ANISOU 1539 C TYR A 204 2246 2266 2298 31 -60 -65 C
ATOM 1540 O TYR A 204 38.066 53.869 67.557 1.00 20.83 O
ANISOU 1540 O TYR A 204 2628 2625 2660 32 -58 -69 O
ATOM 1541 CB TYR A 204 37.742 51.036 68.938 1.00 15.79 C
ANISOU 1541 CB TYR A 204 1965 2006 2027 52 -56 -50 C
ATOM 1542 CG TYR A 204 37.644 49.803 68.108 1.00 14.68 C
ANISOU 1542 CG TYR A 204 1812 1865 1901 55 -53 -44 C
ATOM 1543 CD1 TYR A 204 38.589 48.785 68.212 1.00 14.83 C
ANISOU 1543 CD1 TYR A 204 1818 1892 1925 55 -56 -39 C
ATOM 1544 CD2 TYR A 204 36.559 49.584 67.241 1.00 13.79 C
ANISOU 1544 CD2 TYR A 204 1699 1744 1797 59 -47 -41 C
ATOM 1545 CE1 TYR A 204 38.512 47.686 67.429 1.00 15.25 C
ANISOU 1545 CE1 TYR A 204 1861 1943 1991 58 -52 -34 C
ATOM 1546 CE2 TYR A 204 36.501 48.450 66.472 1.00 13.56 C
ANISOU 1546 CE2 TYR A 204 1659 1714 1781 60 -44 -36 C
ATOM 1547 CZ TYR A 204 37.474 47.497 66.593 1.00 14.89 C
ANISOU 1547 CZ TYR A 204 1817 1889 1953 60 -47 -34 C
ATOM 1548 OH TYR A 204 37.387 46.326 65.823 1.00 18.19 O
ANISOU 1548 OH TYR A 204 2225 2303 2384 62 -43 -30 O
ATOM 1549 N VAL A 205 39.073 52.341 66.243 1.00 19.75 N
ANISOU 1549 N VAL A 205 2467 2496 2539 27 -60 -63 N
ATOM 1550 CA VAL A 205 38.993 53.201 65.077 1.00 21.63 C
ANISOU 1550 CA VAL A 205 2712 2726 2780 19 -58 -67 C
ATOM 1551 C VAL A 205 37.695 52.992 64.280 1.00 18.35 C
ANISOU 1551 C VAL A 205 2298 2303 2372 27 -51 -63 C
ATOM 1552 O VAL A 205 37.244 53.895 63.647 1.00 23.24 O
ANISOU 1552 O VAL A 205 2926 2913 2990 25 -49 -65 O
ATOM 1553 CB VAL A 205 40.130 52.932 64.078 1.00 23.68 C
ANISOU 1553 CB VAL A 205 2961 2991 3046 8 -60 -69 C
ATOM 1554 CG1 VAL A 205 40.060 53.949 62.945 1.00 25.28 C
ANISOU 1554 CG1 VAL A 205 3171 3184 3249 0 -58 -72 C
ATOM 1555 CG2 VAL A 205 41.494 52.992 64.758 1.00 24.69 C
ANISOU 1555 CG2 VAL A 205 3083 3130 3169 0 -67 -72 C
ATOM 1556 N ALA A 206 37.134 51.796 64.316 1.00 15.22 N
ANISOU 1556 N ALA A 206 1891 1909 1982 36 -48 -57 N
ATOM 1557 CA ALA A 206 35.917 51.513 63.515 1.00 14.32 C
ANISOU 1557 CA ALA A 206 1777 1790 1875 42 -43 -52 C
ATOM 1558 C ALA A 206 34.696 52.280 64.012 1.00 13.21 C
ANISOU 1558 C ALA A 206 1646 1643 1729 50 -40 -51 C
ATOM 1559 O ALA A 206 34.585 52.735 65.151 1.00 13.09 O
ANISOU 1559 O ALA A 206 1639 1629 1705 55 -39 -52 O
ATOM 1560 CB ALA A 206 35.667 50.042 63.488 1.00 15.26 C
ANISOU 1560 CB ALA A 206 1883 1913 2002 47 -41 -47 C
ATOM 1561 N THR A 207 33.723 52.393 63.120 1.00 12.23 N
ANISOU 1561 N THR A 207 1523 1515 1609 53 -36 -48 N
ATOM 1562 CA THR A 207 32.534 53.157 63.339 1.00 11.56 C
ANISOU 1562 CA THR A 207 1446 1425 1521 62 -32 -45 C
ATOM 1563 C THR A 207 31.779 52.785 64.624 1.00 11.46 C
ANISOU 1563 C THR A 207 1433 1415 1505 73 -28 -40 C
ATOM 1564 O THR A 207 31.382 51.649 64.823 1.00 11.57 O
ANISOU 1564 O THR A 207 1436 1434 1524 77 -27 -34 O
ATOM 1565 CB THR A 207 31.627 52.977 62.139 1.00 11.13 C
ANISOU 1565 CB THR A 207 1387 1369 1473 64 -30 -40 C
ATOM 1566 OG1 THR A 207 32.400 53.216 60.930 1.00 11.30 O
ANISOU 1566 OG1 THR A 207 1407 1389 1496 53 -33 -44 O
ATOM 1567 CG2 THR A 207 30.469 53.884 62.205 1.00 10.99 C
ANISOU 1567 CG2 THR A 207 1377 1347 1452 73 -26 -37 C
ATOM 1568 N ARG A 208 31.519 53.799 65.464 1.00 10.36 N
ANISOU 1568 N ARG A 208 1306 1272 1356 79 -26 -43 N
ATOM 1569 CA ARG A 208 31.002 53.568 66.794 1.00 10.41 C
ANISOU 1569 CA ARG A 208 1315 1284 1357 89 -22 -40 C
ATOM 1570 C ARG A 208 29.743 52.688 66.856 1.00 10.00 C
ANISOU 1570 C ARG A 208 1252 1236 1311 99 -17 -29 C
ATOM 1571 O ARG A 208 29.661 51.762 67.626 1.00 9.38 O
ANISOU 1571 O ARG A 208 1166 1164 1233 102 -15 -24 O
ATOM 1572 CB ARG A 208 30.719 54.938 67.429 1.00 12.36 C
ANISOU 1572 CB ARG A 208 1580 1524 1594 95 -19 -46 C
ATOM 1573 CG ARG A 208 30.383 54.799 68.881 1.00 12.79 C
ANISOU 1573 CG ARG A 208 1638 1585 1639 104 -16 -44 C
ATOM 1574 CD ARG A 208 29.862 56.089 69.509 1.00 14.22 C
ANISOU 1574 CD ARG A 208 1837 1758 1809 113 -10 -50 C
ATOM 1575 NE ARG A 208 30.811 57.172 69.373 1.00 15.14 N
ANISOU 1575 NE ARG A 208 1967 1865 1920 102 -15 -61 N
ATOM 1576 CZ ARG A 208 30.503 58.360 68.904 1.00 18.21 C
ANISOU 1576 CZ ARG A 208 2370 2241 2308 104 -12 -66 C
ATOM 1577 NH1 ARG A 208 29.246 58.691 68.553 1.00 20.20 N
ANISOU 1577 NH1 ARG A 208 2623 2488 2563 118 -5 -59 N
ATOM 1578 NH2 ARG A 208 31.487 59.276 68.811 1.00 19.79 N
ANISOU 1578 NH2 ARG A 208 2583 2432 2504 91 -18 -76 N
ATOM 1579 N TRP A 209 28.737 53.015 66.049 1.00 9.08 N
ANISOU 1579 N TRP A 209 1134 1117 1200 103 -13 -26 N
ATOM 1580 CA TRP A 209 27.427 52.399 66.187 1.00 9.40 C
ANISOU 1580 CA TRP A 209 1165 1163 1245 113 -8 -16 C
ATOM 1581 C TRP A 209 27.410 50.906 65.892 1.00 8.53 C
ANISOU 1581 C TRP A 209 1039 1058 1145 108 -9 -10 C
ATOM 1582 O TRP A 209 26.462 50.239 66.220 1.00 8.61 O
ANISOU 1582 O TRP A 209 1040 1072 1159 113 -5 -1 O
ATOM 1583 CB TRP A 209 26.426 53.054 65.273 1.00 9.89 C
ANISOU 1583 CB TRP A 209 1227 1221 1310 118 -5 -12 C
ATOM 1584 CG TRP A 209 26.186 54.516 65.560 1.00 10.45 C
ANISOU 1584 CG TRP A 209 1313 1284 1372 126 -1 -16 C
ATOM 1585 CD1 TRP A 209 26.528 55.232 66.681 1.00 11.00 C
ANISOU 1585 CD1 TRP A 209 1398 1351 1432 131 1 -22 C
ATOM 1586 CD2 TRP A 209 25.429 55.405 64.732 1.00 10.95 C
ANISOU 1586 CD2 TRP A 209 1380 1343 1436 132 1 -13 C
ATOM 1587 NE1 TRP A 209 26.062 56.518 66.573 1.00 11.36 N
ANISOU 1587 NE1 TRP A 209 1456 1388 1472 139 5 -24 N
ATOM 1588 CE2 TRP A 209 25.417 56.661 65.378 1.00 11.50 C
ANISOU 1588 CE2 TRP A 209 1467 1404 1497 140 5 -18 C
ATOM 1589 CE3 TRP A 209 24.883 55.303 63.451 1.00 11.16 C
ANISOU 1589 CE3 TRP A 209 1398 1371 1470 130 -2 -8 C
ATOM 1590 CZ2 TRP A 209 24.806 57.760 64.829 1.00 12.72 C
ANISOU 1590 CZ2 TRP A 209 1631 1551 1652 148 8 -16 C
ATOM 1591 CZ3 TRP A 209 24.257 56.417 62.900 1.00 12.48 C
ANISOU 1591 CZ3 TRP A 209 1573 1533 1636 138 1 -5 C
ATOM 1592 CH2 TRP A 209 24.227 57.617 63.575 1.00 12.09 C
ANISOU 1592 CH2 TRP A 209 1540 1474 1579 148 6 -8 C
ATOM 1593 N TYR A 210 28.456 50.413 65.216 1.00 8.41 N
ANISOU 1593 N TYR A 210 1020 1040 1134 96 -15 -15 N
ATOM 1594 CA TYR A 210 28.531 49.006 64.779 1.00 8.56 C
ANISOU 1594 CA TYR A 210 1027 1062 1164 91 -16 -11 C
ATOM 1595 C TYR A 210 29.550 48.192 65.571 1.00 8.33 C
ANISOU 1595 C TYR A 210 996 1036 1135 89 -18 -11 C
ATOM 1596 O TYR A 210 29.785 47.084 65.227 1.00 8.19 O
ANISOU 1596 O TYR A 210 969 1017 1126 85 -19 -9 O
ATOM 1597 CB TYR A 210 28.780 48.934 63.270 1.00 8.76 C
ANISOU 1597 CB TYR A 210 1049 1084 1195 82 -20 -16 C
ATOM 1598 CG TYR A 210 27.712 49.755 62.534 1.00 8.43 C
ANISOU 1598 CG TYR A 210 1008 1041 1152 85 -19 -13 C
ATOM 1599 CD1 TYR A 210 26.482 49.207 62.199 1.00 8.93 C
ANISOU 1599 CD1 TYR A 210 1062 1109 1222 88 -17 -6 C
ATOM 1600 CD2 TYR A 210 27.893 51.104 62.272 1.00 8.65 C
ANISOU 1600 CD2 TYR A 210 1048 1066 1174 86 -20 -17 C
ATOM 1601 CE1 TYR A 210 25.482 49.987 61.653 1.00 8.78 C
ANISOU 1601 CE1 TYR A 210 1043 1091 1201 93 -16 -2 C
ATOM 1602 CE2 TYR A 210 26.891 51.883 61.764 1.00 8.70 C
ANISOU 1602 CE2 TYR A 210 1057 1071 1179 92 -18 -14 C
ATOM 1603 CZ TYR A 210 25.694 51.334 61.434 1.00 8.63 C
ANISOU 1603 CZ TYR A 210 1037 1068 1176 96 -16 -6 C
ATOM 1604 OH TYR A 210 24.660 52.078 60.900 1.00 8.93 O
ANISOU 1604 OH TYR A 210 1074 1107 1212 103 -14 0 O
ATOM 1605 N ARG A 211 30.075 48.774 66.645 1.00 8.27 N
ANISOU 1605 N ARG A 211 996 1030 1117 93 -19 -13 N
ATOM 1606 CA ARG A 211 31.044 48.098 67.532 1.00 9.06 C
ANISOU 1606 CA ARG A 211 1094 1135 1215 92 -21 -12 C
ATOM 1607 C ARG A 211 30.392 47.136 68.476 1.00 8.85 C
ANISOU 1607 C ARG A 211 1061 1113 1189 100 -16 -2 C
ATOM 1608 O ARG A 211 29.489 47.537 69.218 1.00 8.85 O
ANISOU 1608 O ARG A 211 1065 1116 1183 108 -11 3 O
ATOM 1609 CB ARG A 211 31.759 49.153 68.384 1.00 10.48 C
ANISOU 1609 CB ARG A 211 1285 1317 1380 92 -24 -19 C
ATOM 1610 CG ARG A 211 32.657 50.162 67.689 1.00 11.39 C
ANISOU 1610 CG ARG A 211 1407 1427 1492 83 -29 -30 C
ATOM 1611 CD ARG A 211 33.197 51.240 68.653 1.00 11.96 C
ANISOU 1611 CD ARG A 211 1493 1502 1550 82 -32 -37 C
ATOM 1612 NE ARG A 211 33.947 52.232 67.881 1.00 12.87 N
ANISOU 1612 NE ARG A 211 1615 1611 1664 72 -36 -46 N
ATOM 1613 CZ ARG A 211 34.257 53.450 68.346 1.00 13.35 C
ANISOU 1613 CZ ARG A 211 1690 1668 1714 69 -38 -54 C
ATOM 1614 NH1 ARG A 211 33.898 53.839 69.572 1.00 14.21 N
ANISOU 1614 NH1 ARG A 211 1808 1779 1812 76 -36 -55 N
ATOM 1615 NH2 ARG A 211 34.863 54.313 67.519 1.00 13.95 N
ANISOU 1615 NH2 ARG A 211 1772 1738 1791 58 -41 -61 N
ATOM 1616 N ALA A 212 30.902 45.890 68.538 1.00 8.47 N
ANISOU 1616 N ALA A 212 1004 1065 1149 98 -17 3 N
ATOM 1617 CA ALA A 212 30.419 44.912 69.475 1.00 8.48 C
ANISOU 1617 CA ALA A 212 999 1070 1152 104 -12 15 C
ATOM 1618 C ALA A 212 30.701 45.361 70.892 1.00 8.71 C
ANISOU 1618 C ALA A 212 1035 1107 1166 111 -12 17 C
ATOM 1619 O ALA A 212 31.644 46.126 71.155 1.00 7.97 O
ANISOU 1619 O ALA A 212 949 1017 1063 109 -18 9 O
ATOM 1620 CB ALA A 212 31.096 43.609 69.233 1.00 9.22 C
ANISOU 1620 CB ALA A 212 1086 1162 1257 101 -14 19 C
ATOM 1621 N PRO A 213 29.936 44.844 71.852 1.00 8.73 N
ANISOU 1621 N PRO A 213 1036 1115 1167 119 -6 28 N
ATOM 1622 CA PRO A 213 30.126 45.341 73.235 1.00 8.96 C
ANISOU 1622 CA PRO A 213 1073 1154 1179 126 -5 30 C
ATOM 1623 C PRO A 213 31.534 45.079 73.776 1.00 8.61 C
ANISOU 1623 C PRO A 213 1028 1114 1128 124 -13 28 C
ATOM 1624 O PRO A 213 32.082 45.892 74.517 1.00 9.09 O
ANISOU 1624 O PRO A 213 1097 1182 1174 125 -17 22 O
ATOM 1625 CB PRO A 213 29.088 44.566 74.064 1.00 8.96 C
ANISOU 1625 CB PRO A 213 1067 1158 1180 135 3 44 C
ATOM 1626 CG PRO A 213 28.605 43.428 73.153 1.00 8.92 C
ANISOU 1626 CG PRO A 213 1051 1145 1194 130 6 51 C
ATOM 1627 CD PRO A 213 28.788 43.926 71.734 1.00 8.86 C
ANISOU 1627 CD PRO A 213 1043 1128 1194 121 1 40 C
ATOM 1628 N GLU A 214 32.102 43.931 73.423 1.00 8.58 N
ANISOU 1628 N GLU A 214 1015 1109 1137 122 -15 34 N
ATOM 1629 CA GLU A 214 33.419 43.564 73.928 1.00 8.94 C
ANISOU 1629 CA GLU A 214 1058 1161 1178 122 -22 35 C
ATOM 1630 C GLU A 214 34.514 44.538 73.502 1.00 9.03 C
ANISOU 1630 C GLU A 214 1074 1175 1183 114 -30 21 C
ATOM 1631 O GLU A 214 35.553 44.643 74.190 1.00 8.65 O
ANISOU 1631 O GLU A 214 1025 1135 1124 113 -37 20 O
ATOM 1632 CB GLU A 214 33.805 42.131 73.561 1.00 8.95 C
ANISOU 1632 CB GLU A 214 1049 1158 1195 122 -21 44 C
ATOM 1633 CG GLU A 214 33.912 41.816 72.085 1.00 9.32 C
ANISOU 1633 CG GLU A 214 1091 1194 1258 115 -21 38 C
ATOM 1634 CD GLU A 214 32.599 41.397 71.406 1.00 9.31 C
ANISOU 1634 CD GLU A 214 1088 1182 1268 113 -14 41 C
ATOM 1635 OE1 GLU A 214 32.721 40.896 70.239 1.00 9.90 O
ANISOU 1635 OE1 GLU A 214 1157 1247 1356 107 -14 37 O
ATOM 1636 OE2 GLU A 214 31.488 41.591 71.994 1.00 9.65 O
ANISOU 1636 OE2 GLU A 214 1133 1228 1307 117 -9 47 O
ATOM 1637 N ILE A 215 34.324 45.277 72.380 1.00 9.02 N
ANISOU 1637 N ILE A 215 1076 1165 1187 106 -31 11 N
ATOM 1638 CA ILE A 215 35.296 46.314 72.019 1.00 9.34 C
ANISOU 1638 CA ILE A 215 1122 1207 1221 98 -38 -2 C
ATOM 1639 C ILE A 215 35.530 47.306 73.142 1.00 9.40 C
ANISOU 1639 C ILE A 215 1140 1222 1209 99 -42 -7 C
ATOM 1640 O ILE A 215 36.638 47.826 73.312 1.00 9.97 O
ANISOU 1640 O ILE A 215 1214 1301 1275 91 -50 -14 O
ATOM 1641 CB ILE A 215 34.832 47.071 70.747 1.00 10.20 C
ANISOU 1641 CB ILE A 215 1235 1305 1336 92 -36 -11 C
ATOM 1642 CG1 ILE A 215 34.844 46.086 69.590 1.00 11.15 C
ANISOU 1642 CG1 ILE A 215 1345 1419 1473 89 -35 -8 C
ATOM 1643 CG2 ILE A 215 35.672 48.350 70.507 1.00 10.68 C
ANISOU 1643 CG2 ILE A 215 1304 1366 1389 82 -43 -23 C
ATOM 1644 CD1 ILE A 215 36.210 45.573 69.255 1.00 12.46 C
ANISOU 1644 CD1 ILE A 215 1503 1588 1643 84 -40 -10 C
ATOM 1645 N MET A 216 34.482 47.589 73.906 1.00 9.04 N
ANISOU 1645 N MET A 216 1102 1178 1156 107 -35 -4 N
ATOM 1646 CA MET A 216 34.541 48.601 74.974 1.00 9.26 C
ANISOU 1646 CA MET A 216 1142 1212 1165 108 -37 -11 C
ATOM 1647 C MET A 216 35.022 48.014 76.304 1.00 9.25 C
ANISOU 1647 C MET A 216 1138 1225 1152 114 -40 -3 C
ATOM 1648 O MET A 216 35.267 48.742 77.251 1.00 9.53 O
ANISOU 1648 O MET A 216 1184 1268 1170 114 -43 -9 O
ATOM 1649 CB MET A 216 33.189 49.304 75.117 1.00 9.86 C
ANISOU 1649 CB MET A 216 1228 1282 1237 116 -28 -12 C
ATOM 1650 CG MET A 216 32.912 50.333 73.995 1.00 9.97 C
ANISOU 1650 CG MET A 216 1249 1283 1257 110 -27 -22 C
ATOM 1651 SD MET A 216 32.442 49.589 72.429 1.00 9.72 S
ANISOU 1651 SD MET A 216 1205 1243 1247 107 -25 -17 S
ATOM 1652 CE MET A 216 30.802 49.123 72.762 1.00 10.41 C
ANISOU 1652 CE MET A 216 1288 1330 1337 120 -14 -5 C
ATOM 1653 N LEU A 217 35.112 46.693 76.380 1.00 9.49 N
ANISOU 1653 N LEU A 217 1156 1258 1192 118 -39 10 N
ATOM 1654 CA LEU A 217 35.372 45.934 77.610 1.00 9.67 C
ANISOU 1654 CA LEU A 217 1175 1294 1205 126 -40 22 C
ATOM 1655 C LEU A 217 36.702 45.284 77.630 1.00 9.58 C
ANISOU 1655 C LEU A 217 1154 1291 1196 122 -49 26 C
ATOM 1656 O LEU A 217 37.430 45.434 78.593 1.00 10.11 O
ANISOU 1656 O LEU A 217 1221 1371 1247 123 -56 26 O
ATOM 1657 CB LEU A 217 34.309 44.884 77.791 1.00 9.61 C
ANISOU 1657 CB LEU A 217 1162 1284 1207 135 -30 38 C
ATOM 1658 CG LEU A 217 32.896 45.486 77.989 1.00 9.79 C
ANISOU 1658 CG LEU A 217 1192 1302 1224 141 -20 37 C
ATOM 1659 CD1 LEU A 217 31.856 44.377 77.868 1.00 9.48 C
ANISOU 1659 CD1 LEU A 217 1144 1259 1199 147 -10 52 C
ATOM 1660 CD2 LEU A 217 32.686 46.238 79.303 1.00 10.02 C
ANISOU 1660 CD2 LEU A 217 1233 1344 1231 147 -18 34 C
ATOM 1661 N ASN A 218 37.033 44.538 76.572 1.00 9.29 N
ANISOU 1661 N ASN A 218 1107 1246 1178 120 -49 28 N
ATOM 1662 CA ASN A 218 38.221 43.663 76.640 1.00 9.25 C
ANISOU 1662 CA ASN A 218 1089 1247 1177 121 -55 36 C
ATOM 1663 C ASN A 218 38.782 43.143 75.299 1.00 9.21 C
ANISOU 1663 C ASN A 218 1076 1234 1191 116 -55 33 C
ATOM 1664 O ASN A 218 39.610 42.234 75.275 1.00 9.06 O
ANISOU 1664 O ASN A 218 1046 1218 1179 119 -58 41 O
ATOM 1665 CB ASN A 218 37.969 42.463 77.577 1.00 9.46 C
ANISOU 1665 CB ASN A 218 1111 1280 1204 132 -51 54 C
ATOM 1666 CG ASN A 218 36.974 41.496 77.004 1.00 10.84 C
ANISOU 1666 CG ASN A 218 1282 1441 1397 137 -40 63 C
ATOM 1667 OD1 ASN A 218 36.415 41.735 75.940 1.00 11.24 O
ANISOU 1667 OD1 ASN A 218 1333 1478 1458 131 -36 56 O
ATOM 1668 ND2 ASN A 218 36.771 40.393 77.686 1.00 11.47 N
ANISOU 1668 ND2 ASN A 218 1357 1522 1479 146 -36 80 N
ATOM 1669 N SER A 219 38.384 43.750 74.186 1.00 9.26 N
ANISOU 1669 N SER A 219 1085 1227 1204 108 -53 22 N
ATOM 1670 CA SER A 219 38.675 43.128 72.891 1.00 9.42 C
ANISOU 1670 CA SER A 219 1098 1239 1243 105 -51 21 C
ATOM 1671 C SER A 219 39.179 44.171 71.915 1.00 9.79 C
ANISOU 1671 C SER A 219 1147 1282 1289 93 -55 6 C
ATOM 1672 O SER A 219 38.616 45.222 71.779 1.00 10.03 O
ANISOU 1672 O SER A 219 1188 1309 1313 89 -54 -2 O
ATOM 1673 CB SER A 219 37.439 42.453 72.268 1.00 9.46 C
ANISOU 1673 CB SER A 219 1103 1229 1261 108 -41 25 C
ATOM 1674 OG SER A 219 37.757 41.891 70.986 1.00 10.02 O
ANISOU 1674 OG SER A 219 1168 1292 1348 104 -40 22 O
ATOM 1675 N LYS A 220 40.228 43.791 71.192 1.00 10.05 N
ANISOU 1675 N LYS A 220 1171 1317 1329 90 -58 4 N
ATOM 1676 CA LYS A 220 40.755 44.570 70.106 1.00 10.97 C
ANISOU 1676 CA LYS A 220 1288 1431 1449 79 -60 -8 C
ATOM 1677 C LYS A 220 39.993 44.316 68.792 1.00 10.61 C
ANISOU 1677 C LYS A 220 1244 1371 1416 77 -53 -11 C
ATOM 1678 O LYS A 220 40.379 44.928 67.755 1.00 11.59 O
ANISOU 1678 O LYS A 220 1369 1493 1542 68 -54 -20 O
ATOM 1679 CB LYS A 220 42.252 44.195 69.909 1.00 13.20 C
ANISOU 1679 CB LYS A 220 1558 1723 1733 77 -66 -7 C
ATOM 1680 CG LYS A 220 43.187 44.601 71.018 1.00 15.52 C
ANISOU 1680 CG LYS A 220 1850 2034 2014 75 -75 -6 C
ATOM 1681 CD LYS A 220 44.618 44.203 70.670 1.00 20.30 C
ANISOU 1681 CD LYS A 220 2439 2649 2623 73 -79 -4 C
ATOM 1682 CE LYS A 220 45.614 44.210 71.812 1.00 25.83 C
ANISOU 1682 CE LYS A 220 3132 3370 3312 75 -89 1 C
ATOM 1683 NZ LYS A 220 46.685 43.194 71.493 1.00 27.44 N
ANISOU 1683 NZ LYS A 220 3319 3582 3527 81 -89 9 N
ATOM 1684 N GLY A 221 39.052 43.373 68.741 1.00 9.89 N
ANISOU 1684 N GLY A 221 1152 1272 1334 84 -46 -4 N
ATOM 1685 CA GLY A 221 38.355 43.063 67.480 1.00 9.65 C
ANISOU 1685 CA GLY A 221 1122 1230 1316 82 -41 -7 C
ATOM 1686 C GLY A 221 39.167 42.236 66.534 1.00 10.02 C
ANISOU 1686 C GLY A 221 1160 1273 1374 81 -40 -9 C
ATOM 1687 O GLY A 221 39.089 42.472 65.309 1.00 11.78 O
ANISOU 1687 O GLY A 221 1383 1491 1601 74 -38 -17 O
ATOM 1688 N TYR A 222 39.883 41.253 67.061 1.00 9.75 N
ANISOU 1688 N TYR A 222 1118 1243 1344 88 -40 -1 N
ATOM 1689 CA TYR A 222 40.729 40.380 66.233 1.00 9.66 C
ANISOU 1689 CA TYR A 222 1098 1229 1344 90 -37 -2 C
ATOM 1690 C TYR A 222 40.131 38.989 66.034 1.00 9.57 C
ANISOU 1690 C TYR A 222 1085 1204 1346 97 -30 4 C
ATOM 1691 O TYR A 222 40.841 38.017 65.727 1.00 9.71 O
ANISOU 1691 O TYR A 222 1097 1220 1374 103 -27 6 O
ATOM 1692 CB TYR A 222 42.138 40.241 66.826 1.00 10.55 C
ANISOU 1692 CB TYR A 222 1202 1355 1453 94 -42 2 C
ATOM 1693 CG TYR A 222 42.975 41.497 66.897 1.00 10.76 C
ANISOU 1693 CG TYR A 222 1227 1394 1467 85 -50 -5 C
ATOM 1694 CD1 TYR A 222 42.643 42.646 66.230 1.00 11.88 C
ANISOU 1694 CD1 TYR A 222 1376 1533 1603 74 -51 -16 C
ATOM 1695 CD2 TYR A 222 44.194 41.449 67.522 1.00 11.71 C
ANISOU 1695 CD2 TYR A 222 1337 1528 1582 88 -56 -1 C
ATOM 1696 CE1 TYR A 222 43.443 43.779 66.278 1.00 13.44 C
ANISOU 1696 CE1 TYR A 222 1575 1741 1792 64 -57 -22 C
ATOM 1697 CE2 TYR A 222 45.007 42.555 67.551 1.00 12.61 C
ANISOU 1697 CE2 TYR A 222 1451 1655 1687 77 -63 -8 C
ATOM 1698 CZ TYR A 222 44.630 43.718 66.960 1.00 13.45 C
ANISOU 1698 CZ TYR A 222 1566 1757 1788 65 -64 -18 C
ATOM 1699 OH TYR A 222 45.502 44.815 67.011 1.00 16.57 O
ANISOU 1699 OH TYR A 222 1960 2162 2174 53 -71 -25 O
ATOM 1700 N THR A 223 38.790 38.834 66.185 1.00 9.22 N
ANISOU 1700 N THR A 223 1047 1152 1304 97 -27 7 N
ATOM 1701 CA THR A 223 38.163 37.536 65.905 1.00 9.62 C
ANISOU 1701 CA THR A 223 1098 1190 1370 100 -20 12 C
ATOM 1702 C THR A 223 36.931 37.745 65.032 1.00 9.02 C
ANISOU 1702 C THR A 223 1026 1104 1296 92 -17 6 C
ATOM 1703 O THR A 223 36.406 38.866 64.954 1.00 8.87 O
ANISOU 1703 O THR A 223 1011 1090 1268 86 -20 1 O
ATOM 1704 CB THR A 223 37.755 36.788 67.174 1.00 10.66 C
ANISOU 1704 CB THR A 223 1228 1320 1502 109 -17 27 C
ATOM 1705 OG1 THR A 223 36.697 37.430 67.822 1.00 11.63 O
ANISOU 1705 OG1 THR A 223 1356 1446 1617 107 -18 31 O
ATOM 1706 CG2 THR A 223 38.929 36.699 68.120 1.00 11.29 C
ANISOU 1706 CG2 THR A 223 1303 1412 1576 117 -21 35 C
ATOM 1707 N LYS A 224 36.491 36.682 64.382 1.00 8.79 N
ANISOU 1707 N LYS A 224 997 1063 1281 91 -12 5 N
ATOM 1708 CA LYS A 224 35.439 36.771 63.400 1.00 8.47 C
ANISOU 1708 CA LYS A 224 960 1015 1244 82 -11 -2 C
ATOM 1709 C LYS A 224 34.094 37.250 63.962 1.00 8.18 C
ANISOU 1709 C LYS A 224 925 981 1203 80 -11 4 C
ATOM 1710 O LYS A 224 33.290 37.892 63.253 1.00 8.15 O
ANISOU 1710 O LYS A 224 924 978 1197 72 -12 -2 O
ATOM 1711 CB LYS A 224 35.317 35.458 62.657 1.00 8.66 C
ANISOU 1711 CB LYS A 224 983 1024 1282 80 -5 -5 C
ATOM 1712 CG LYS A 224 36.522 35.193 61.750 1.00 9.00 C
ANISOU 1712 CG LYS A 224 1025 1066 1329 82 -5 -14 C
ATOM 1713 CD LYS A 224 36.579 33.792 61.183 1.00 9.41 C
ANISOU 1713 CD LYS A 224 1077 1102 1395 83 2 -17 C
ATOM 1714 CE LYS A 224 37.847 33.640 60.381 1.00 9.37 C
ANISOU 1714 CE LYS A 224 1071 1098 1391 87 4 -26 C
ATOM 1715 NZ LYS A 224 37.988 32.272 59.840 1.00 9.37 N
ANISOU 1715 NZ LYS A 224 1073 1081 1405 90 11 -30 N
ATOM 1716 N SER A 225 33.895 37.022 65.246 1.00 8.34 N
ANISOU 1716 N SER A 225 945 1004 1221 87 -9 16 N
ATOM 1717 CA SER A 225 32.708 37.500 65.917 1.00 8.31 C
ANISOU 1717 CA SER A 225 942 1004 1212 87 -8 23 C
ATOM 1718 C SER A 225 32.483 39.009 65.806 1.00 8.11 C
ANISOU 1718 C SER A 225 920 987 1172 84 -12 16 C
ATOM 1719 O SER A 225 31.343 39.461 65.961 1.00 8.43 O
ANISOU 1719 O SER A 225 963 1031 1211 83 -10 19 O
ATOM 1720 CB SER A 225 32.773 37.062 67.393 1.00 8.73 C
ANISOU 1720 CB SER A 225 994 1061 1262 96 -6 38 C
ATOM 1721 OG SER A 225 33.900 37.642 68.027 1.00 10.49 O
ANISOU 1721 OG SER A 225 1218 1294 1474 101 -10 37 O
ATOM 1722 N ILE A 226 33.550 39.789 65.601 1.00 8.09 N
ANISOU 1722 N ILE A 226 920 990 1162 84 -17 8 N
ATOM 1723 CA ILE A 226 33.423 41.220 65.493 1.00 8.92 C
ANISOU 1723 CA ILE A 226 1030 1102 1256 81 -20 2 C
ATOM 1724 C ILE A 226 32.559 41.604 64.295 1.00 8.30 C
ANISOU 1724 C ILE A 226 954 1020 1181 74 -20 -5 C
ATOM 1725 O ILE A 226 31.736 42.532 64.377 1.00 8.22 O
ANISOU 1725 O ILE A 226 947 1012 1164 74 -20 -5 O
ATOM 1726 CB ILE A 226 34.815 41.920 65.414 1.00 9.87 C
ANISOU 1726 CB ILE A 226 1153 1229 1369 79 -25 -6 C
ATOM 1727 CG1 ILE A 226 34.687 43.372 65.748 1.00 12.25 C
ANISOU 1727 CG1 ILE A 226 1461 1535 1657 77 -28 -10 C
ATOM 1728 CG2 ILE A 226 35.524 41.760 64.083 1.00 10.64 C
ANISOU 1728 CG2 ILE A 226 1248 1323 1473 73 -26 -15 C
ATOM 1729 CD1 ILE A 226 34.334 43.580 67.164 1.00 13.81 C
ANISOU 1729 CD1 ILE A 226 1662 1739 1846 85 -28 -2 C
ATOM 1730 N ASP A 227 32.717 40.883 63.189 1.00 7.79 N
ANISOU 1730 N ASP A 227 886 948 1125 68 -19 -10 N
ATOM 1731 CA ASP A 227 31.984 41.204 61.998 1.00 7.50 C
ANISOU 1731 CA ASP A 227 850 910 1091 61 -20 -16 C
ATOM 1732 C ASP A 227 30.543 40.713 62.079 1.00 7.46 C
ANISOU 1732 C ASP A 227 841 901 1091 60 -17 -9 C
ATOM 1733 O ASP A 227 29.616 41.353 61.559 1.00 7.63 O
ANISOU 1733 O ASP A 227 863 926 1109 58 -18 -10 O
ATOM 1734 CB ASP A 227 32.667 40.549 60.791 1.00 7.39 C
ANISOU 1734 CB ASP A 227 834 891 1083 56 -20 -25 C
ATOM 1735 CG ASP A 227 33.946 41.268 60.342 1.00 7.51 C
ANISOU 1735 CG ASP A 227 851 910 1091 54 -23 -33 C
ATOM 1736 OD1 ASP A 227 34.061 42.494 60.514 1.00 7.09 O
ANISOU 1736 OD1 ASP A 227 802 863 1028 53 -26 -34 O
ATOM 1737 OD2 ASP A 227 34.772 40.565 59.691 1.00 8.26 O
ANISOU 1737 OD2 ASP A 227 943 1002 1192 53 -21 -38 O
ATOM 1738 N ILE A 228 30.330 39.581 62.720 1.00 7.96 N
ANISOU 1738 N ILE A 228 901 960 1163 63 -13 -2 N
ATOM 1739 CA ILE A 228 28.978 39.094 62.903 1.00 8.54 C
ANISOU 1739 CA ILE A 228 970 1032 1242 61 -10 6 C
ATOM 1740 C ILE A 228 28.114 40.062 63.708 1.00 8.18 C
ANISOU 1740 C ILE A 228 926 996 1188 67 -9 13 C
ATOM 1741 O ILE A 228 26.951 40.352 63.346 1.00 7.89 O
ANISOU 1741 O ILE A 228 886 962 1152 64 -9 15 O
ATOM 1742 CB ILE A 228 28.977 37.684 63.502 1.00 9.14 C
ANISOU 1742 CB ILE A 228 1043 1100 1329 62 -6 15 C
ATOM 1743 CG1 ILE A 228 29.681 36.700 62.547 1.00 10.10 C
ANISOU 1743 CG1 ILE A 228 1165 1211 1461 57 -6 6 C
ATOM 1744 CG2 ILE A 228 27.557 37.199 63.794 1.00 9.35 C
ANISOU 1744 CG2 ILE A 228 1064 1125 1362 59 -2 24 C
ATOM 1745 CD1 ILE A 228 28.918 36.360 61.291 1.00 11.46 C
ANISOU 1745 CD1 ILE A 228 1336 1378 1640 45 -7 -2 C
ATOM 1746 N TRP A 229 28.687 40.655 64.741 1.00 8.09 N
ANISOU 1746 N TRP A 229 918 989 1167 75 -9 16 N
ATOM 1747 CA TRP A 229 27.977 41.688 65.488 1.00 7.59 C
ANISOU 1747 CA TRP A 229 858 934 1093 81 -7 20 C
ATOM 1748 C TRP A 229 27.518 42.828 64.552 1.00 7.75 C
ANISOU 1748 C TRP A 229 881 957 1109 79 -10 13 C
ATOM 1749 O TRP A 229 26.365 43.236 64.582 1.00 7.80 O
ANISOU 1749 O TRP A 229 885 966 1113 81 -7 18 O
ATOM 1750 CB TRP A 229 28.854 42.275 66.606 1.00 7.81 C
ANISOU 1750 CB TRP A 229 892 966 1109 89 -8 21 C
ATOM 1751 CG TRP A 229 28.124 43.343 67.354 1.00 7.34 C
ANISOU 1751 CG TRP A 229 837 914 1038 96 -5 24 C
ATOM 1752 CD1 TRP A 229 28.087 44.703 67.048 1.00 7.59 C
ANISOU 1752 CD1 TRP A 229 876 947 1060 97 -7 16 C
ATOM 1753 CD2 TRP A 229 27.248 43.195 68.474 1.00 7.65 C
ANISOU 1753 CD2 TRP A 229 874 958 1073 104 1 35 C
ATOM 1754 NE1 TRP A 229 27.267 45.349 67.872 1.00 7.51 N
ANISOU 1754 NE1 TRP A 229 869 941 1042 105 -3 21 N
ATOM 1755 CE2 TRP A 229 26.726 44.471 68.755 1.00 7.60 C
ANISOU 1755 CE2 TRP A 229 875 957 1057 110 3 32 C
ATOM 1756 CE3 TRP A 229 26.820 42.101 69.257 1.00 7.89 C
ANISOU 1756 CE3 TRP A 229 899 990 1110 106 6 47 C
ATOM 1757 CZ2 TRP A 229 25.802 44.702 69.763 1.00 7.95 C
ANISOU 1757 CZ2 TRP A 229 920 1008 1095 119 10 40 C
ATOM 1758 CZ3 TRP A 229 25.908 42.355 70.292 1.00 8.29 C
ANISOU 1758 CZ3 TRP A 229 949 1048 1153 115 13 57 C
ATOM 1759 CH2 TRP A 229 25.423 43.657 70.528 1.00 8.42 C
ANISOU 1759 CH2 TRP A 229 972 1070 1158 122 15 53 C
ATOM 1760 N SER A 230 28.453 43.316 63.735 1.00 7.37 N
ANISOU 1760 N SER A 230 837 906 1057 74 -15 3 N
ATOM 1761 CA SER A 230 28.113 44.425 62.848 1.00 7.23 C
ANISOU 1761 CA SER A 230 823 890 1035 72 -17 -3 C
ATOM 1762 C SER A 230 27.016 44.031 61.870 1.00 7.15 C
ANISOU 1762 C SER A 230 806 880 1032 67 -17 -1 C
ATOM 1763 O SER A 230 26.135 44.781 61.564 1.00 7.09 O
ANISOU 1763 O SER A 230 798 876 1021 69 -17 1 O
ATOM 1764 CB SER A 230 29.338 44.882 62.048 1.00 7.64 C
ANISOU 1764 CB SER A 230 880 940 1084 66 -22 -13 C
ATOM 1765 OG SER A 230 30.401 45.278 62.931 1.00 8.82 O
ANISOU 1765 OG SER A 230 1034 1090 1226 69 -23 -15 O
ATOM 1766 N VAL A 231 27.056 42.824 61.371 1.00 6.75 N
ANISOU 1766 N VAL A 231 749 825 991 60 -18 -2 N
ATOM 1767 CA VAL A 231 25.979 42.325 60.508 1.00 7.45 C
ANISOU 1767 CA VAL A 231 831 914 1087 53 -19 -1 C
ATOM 1768 C VAL A 231 24.661 42.342 61.222 1.00 7.48 C
ANISOU 1768 C VAL A 231 827 922 1091 57 -15 10 C
ATOM 1769 O VAL A 231 23.643 42.716 60.641 1.00 7.74 O
ANISOU 1769 O VAL A 231 855 961 1123 55 -16 12 O
ATOM 1770 CB VAL A 231 26.267 40.945 59.891 1.00 7.83 C
ANISOU 1770 CB VAL A 231 875 954 1145 43 -19 -6 C
ATOM 1771 CG1 VAL A 231 25.061 40.476 59.052 1.00 8.04 C
ANISOU 1771 CG1 VAL A 231 894 982 1177 34 -21 -5 C
ATOM 1772 CG2 VAL A 231 27.505 41.031 59.015 1.00 8.33 C
ANISOU 1772 CG2 VAL A 231 944 1015 1207 40 -22 -18 C
ATOM 1773 N GLY A 232 24.641 41.875 62.447 1.00 7.58 N
ANISOU 1773 N GLY A 232 839 935 1105 63 -10 18 N
ATOM 1774 CA GLY A 232 23.404 41.934 63.253 1.00 7.61 C
ANISOU 1774 CA GLY A 232 837 945 1109 68 -5 30 C
ATOM 1775 C GLY A 232 22.875 43.342 63.396 1.00 7.72 C
ANISOU 1775 C GLY A 232 854 967 1113 78 -4 31 C
ATOM 1776 O GLY A 232 21.690 43.617 63.204 1.00 7.85 O
ANISOU 1776 O GLY A 232 863 990 1130 79 -2 37 O
ATOM 1777 N CYS A 233 23.784 44.294 63.604 1.00 7.24 N
ANISOU 1777 N CYS A 233 804 905 1042 83 -5 25 N
ATOM 1778 CA CYS A 233 23.391 45.727 63.633 1.00 7.87 C
ANISOU 1778 CA CYS A 233 890 989 1112 92 -5 24 C
ATOM 1779 C CYS A 233 22.776 46.185 62.302 1.00 7.69 C
ANISOU 1779 C CYS A 233 864 968 1091 88 -9 22 C
ATOM 1780 O CYS A 233 21.790 46.954 62.261 1.00 8.04 O
ANISOU 1780 O CYS A 233 905 1018 1131 95 -7 27 O
ATOM 1781 CB CYS A 233 24.560 46.641 63.941 1.00 8.05 C
ANISOU 1781 CB CYS A 233 927 1008 1125 95 -6 16 C
ATOM 1782 SG CYS A 233 25.203 46.426 65.628 1.00 9.33 S
ANISOU 1782 SG CYS A 233 1094 1170 1281 102 -2 19 S
ATOM 1783 N ILE A 234 23.349 45.704 61.191 1.00 7.81 N
ANISOU 1783 N ILE A 234 878 979 1110 76 -15 14 N
ATOM 1784 CA ILE A 234 22.844 46.027 59.858 1.00 7.78 C
ANISOU 1784 CA ILE A 234 871 979 1107 71 -19 12 C
ATOM 1785 C ILE A 234 21.476 45.409 59.642 1.00 7.45 C
ANISOU 1785 C ILE A 234 814 944 1071 68 -19 20 C
ATOM 1786 O ILE A 234 20.593 46.053 59.054 1.00 8.81 O
ANISOU 1786 O ILE A 234 982 1124 1241 71 -21 24 O
ATOM 1787 CB ILE A 234 23.823 45.610 58.778 1.00 8.10 C
ANISOU 1787 CB ILE A 234 914 1014 1149 60 -25 2 C
ATOM 1788 CG1 ILE A 234 25.108 46.476 58.889 1.00 7.93 C
ANISOU 1788 CG1 ILE A 234 905 988 1120 62 -25 -6 C
ATOM 1789 CG2 ILE A 234 23.246 45.789 57.379 1.00 8.09 C
ANISOU 1789 CG2 ILE A 234 908 1018 1147 53 -30 0 C
ATOM 1790 CD1 ILE A 234 26.343 45.862 58.282 1.00 8.70 C
ANISOU 1790 CD1 ILE A 234 1005 1081 1221 53 -28 -15 C
ATOM 1791 N LEU A 235 21.294 44.155 60.041 1.00 7.51 N
ANISOU 1791 N LEU A 235 815 950 1089 62 -17 23 N
ATOM 1792 CA LEU A 235 19.978 43.561 59.934 1.00 7.92 C
ANISOU 1792 CA LEU A 235 853 1010 1148 58 -17 32 C
ATOM 1793 C LEU A 235 18.928 44.346 60.690 1.00 8.32 C
ANISOU 1793 C LEU A 235 898 1069 1193 71 -11 44 C
ATOM 1794 O LEU A 235 17.841 44.652 60.156 1.00 8.35 O
ANISOU 1794 O LEU A 235 892 1083 1197 71 -13 49 O
ATOM 1795 CB LEU A 235 20.060 42.116 60.427 1.00 8.04 C
ANISOU 1795 CB LEU A 235 864 1019 1173 50 -14 34 C
ATOM 1796 CG LEU A 235 18.704 41.379 60.502 1.00 8.55 C
ANISOU 1796 CG LEU A 235 913 1090 1246 43 -13 44 C
ATOM 1797 CD1 LEU A 235 18.018 41.351 59.120 1.00 9.09 C
ANISOU 1797 CD1 LEU A 235 973 1164 1316 32 -21 41 C
ATOM 1798 CD2 LEU A 235 18.949 39.936 61.005 1.00 9.55 C
ANISOU 1798 CD2 LEU A 235 1037 1206 1384 35 -9 46 C
ATOM 1799 N ALA A 236 19.217 44.712 61.926 1.00 8.35 N
ANISOU 1799 N ALA A 236 909 1072 1193 82 -4 47 N
ATOM 1800 CA ALA A 236 18.282 45.506 62.736 1.00 9.01 C
ANISOU 1800 CA ALA A 236 989 1164 1270 97 3 57 C
ATOM 1801 C ALA A 236 17.911 46.802 62.028 1.00 9.12 C
ANISOU 1801 C ALA A 236 1006 1182 1277 105 0 56 C
ATOM 1802 O ALA A 236 16.773 47.241 61.997 1.00 9.01 O
ANISOU 1802 O ALA A 236 983 1178 1263 112 3 65 O
ATOM 1803 CB ALA A 236 18.884 45.787 64.127 1.00 9.32 C
ANISOU 1803 CB ALA A 236 1039 1199 1302 107 10 58 C
ATOM 1804 N GLU A 237 18.907 47.433 61.466 1.00 8.98 N
ANISOU 1804 N GLU A 237 1001 1157 1255 103 -4 46 N
ATOM 1805 CA GLU A 237 18.725 48.675 60.772 1.00 9.55 C
ANISOU 1805 CA GLU A 237 1079 1230 1321 110 -7 45 C
ATOM 1806 C GLU A 237 17.885 48.486 59.502 1.00 9.38 C
ANISOU 1806 C GLU A 237 1044 1217 1302 103 -13 48 C
ATOM 1807 O GLU A 237 17.065 49.370 59.146 1.00 9.52 O
ANISOU 1807 O GLU A 237 1058 1241 1316 113 -13 55 O
ATOM 1808 CB GLU A 237 20.087 49.293 60.487 1.00 9.94 C
ANISOU 1808 CB GLU A 237 1144 1268 1363 107 -10 33 C
ATOM 1809 CG GLU A 237 20.076 50.695 59.987 1.00 10.56 C
ANISOU 1809 CG GLU A 237 1233 1345 1435 116 -11 32 C
ATOM 1810 CD GLU A 237 21.364 51.466 60.247 1.00 10.39 C
ANISOU 1810 CD GLU A 237 1229 1312 1407 116 -11 23 C
ATOM 1811 OE1 GLU A 237 22.311 51.022 60.945 1.00 10.20 O
ANISOU 1811 OE1 GLU A 237 1210 1283 1382 111 -10 17 O
ATOM 1812 OE2 GLU A 237 21.446 52.591 59.723 1.00 12.51 O
ANISOU 1812 OE2 GLU A 237 1507 1576 1670 120 -11 22 O
ATOM 1813 N MET A 238 18.018 47.362 58.803 1.00 8.92 N
ANISOU 1813 N MET A 238 979 1160 1252 87 -19 44 N
ATOM 1814 CA MET A 238 17.171 47.062 57.633 1.00 9.86 C
ANISOU 1814 CA MET A 238 1085 1288 1373 78 -26 47 C
ATOM 1815 C MET A 238 15.721 46.822 58.057 1.00 10.51 C
ANISOU 1815 C MET A 238 1150 1384 1460 83 -23 60 C
ATOM 1816 O MET A 238 14.808 47.169 57.306 1.00 11.53 O
ANISOU 1816 O MET A 238 1267 1524 1588 83 -27 66 O
ATOM 1817 CB MET A 238 17.671 45.837 56.867 1.00 9.31 C
ANISOU 1817 CB MET A 238 1013 1215 1310 60 -33 38 C
ATOM 1818 CG MET A 238 18.959 46.064 56.081 1.00 9.32 C
ANISOU 1818 CG MET A 238 1027 1207 1306 54 -37 25 C
ATOM 1819 SD MET A 238 19.318 44.864 54.819 1.00 9.89 S
ANISOU 1819 SD MET A 238 1097 1278 1383 34 -45 13 S
ATOM 1820 CE MET A 238 19.848 43.501 55.794 1.00 9.99 C
ANISOU 1820 CE MET A 238 1110 1280 1407 29 -39 11 C
ATOM 1821 N LEU A 239 15.532 46.277 59.257 1.00 10.07 N
ANISOU 1821 N LEU A 239 1091 1327 1409 86 -15 66 N
ATOM 1822 CA LEU A 239 14.182 45.972 59.776 1.00 11.29 C
ANISOU 1822 CA LEU A 239 1227 1494 1568 89 -10 79 C
ATOM 1823 C LEU A 239 13.466 47.256 60.126 1.00 12.00 C
ANISOU 1823 C LEU A 239 1316 1592 1650 109 -5 88 C
ATOM 1824 O LEU A 239 12.247 47.335 59.932 1.00 14.00 O
ANISOU 1824 O LEU A 239 1553 1861 1906 113 -4 99 O
ATOM 1825 CB LEU A 239 14.249 45.054 60.959 1.00 11.54 C
ANISOU 1825 CB LEU A 239 1257 1522 1605 87 -3 84 C
ATOM 1826 CG LEU A 239 14.731 43.622 60.662 1.00 12.32 C
ANISOU 1826 CG LEU A 239 1354 1612 1714 67 -7 77 C
ATOM 1827 CD1 LEU A 239 15.009 42.943 61.979 1.00 14.97 C
ANISOU 1827 CD1 LEU A 239 1693 1943 2054 70 2 82 C
ATOM 1828 CD2 LEU A 239 13.851 42.769 59.801 1.00 13.52 C
ANISOU 1828 CD2 LEU A 239 1490 1772 1874 51 -14 80 C
ATOM 1829 N SER A 240 14.173 48.244 60.649 1.00 12.20 N
ANISOU 1829 N SER A 240 1359 1609 1668 123 0 84 N
ATOM 1830 CA SER A 240 13.511 49.427 61.260 1.00 12.22 C
ANISOU 1830 CA SER A 240 1364 1617 1664 145 9 92 C
ATOM 1831 C SER A 240 13.841 50.763 60.634 1.00 11.24 C
ANISOU 1831 C SER A 240 1252 1486 1531 155 6 88 C
ATOM 1832 O SER A 240 13.290 51.780 61.041 1.00 11.86 O
ANISOU 1832 O SER A 240 1334 1568 1606 173 13 94 O
ATOM 1833 CB SER A 240 13.931 49.505 62.732 1.00 13.69 C
ANISOU 1833 CB SER A 240 1560 1796 1846 154 19 91 C
ATOM 1834 OG SER A 240 15.338 49.732 62.805 1.00 16.77 O
ANISOU 1834 OG SER A 240 1970 2171 2231 150 16 78 O
ATOM 1835 N ASN A 241 14.771 50.793 59.678 1.00 10.65 N
ANISOU 1835 N ASN A 241 1188 1404 1456 143 -3 78 N
ATOM 1836 CA ASN A 241 15.266 52.018 59.075 1.00 11.43 C
ANISOU 1836 CA ASN A 241 1301 1495 1548 150 -5 73 C
ATOM 1837 C ASN A 241 15.887 53.002 60.074 1.00 12.42 C
ANISOU 1837 C ASN A 241 1446 1608 1666 164 4 69 C
ATOM 1838 O ASN A 241 15.865 54.188 59.844 1.00 14.64 O
ANISOU 1838 O ASN A 241 1737 1883 1941 175 5 70 O
ATOM 1839 CB ASN A 241 14.167 52.715 58.283 1.00 11.68 C
ANISOU 1839 CB ASN A 241 1322 1538 1578 160 -7 84 C
ATOM 1840 CG ASN A 241 13.762 51.942 57.045 1.00 11.35 C
ANISOU 1840 CG ASN A 241 1264 1508 1540 144 -18 86 C
ATOM 1841 OD1 ASN A 241 12.923 51.063 57.114 1.00 12.55 O
ANISOU 1841 OD1 ASN A 241 1398 1672 1698 138 -19 92 O
ATOM 1842 ND2 ASN A 241 14.329 52.268 55.933 1.00 10.98 N
ANISOU 1842 ND2 ASN A 241 1224 1458 1489 137 -26 80 N
ATOM 1843 N ARG A 242 16.458 52.512 61.158 1.00 12.39 N
ANISOU 1843 N ARG A 242 1447 1598 1661 162 8 64 N
ATOM 1844 CA ARG A 242 17.253 53.346 62.041 1.00 13.03 C
ANISOU 1844 CA ARG A 242 1548 1668 1735 170 14 57 C
ATOM 1845 C ARG A 242 18.310 52.503 62.710 1.00 12.23 C
ANISOU 1845 C ARG A 242 1452 1561 1634 159 13 48 C
ATOM 1846 O ARG A 242 18.152 51.316 62.863 1.00 11.20 O
ANISOU 1846 O ARG A 242 1309 1436 1510 150 12 51 O
ATOM 1847 CB ARG A 242 16.397 54.020 63.115 1.00 17.09 C
ANISOU 1847 CB ARG A 242 2064 2185 2244 191 25 64 C
ATOM 1848 CG ARG A 242 15.682 53.018 64.000 1.00 20.74 C
ANISOU 1848 CG ARG A 242 2510 2658 2710 192 31 72 C
ATOM 1849 CD ARG A 242 14.831 53.667 65.107 1.00 28.34 C
ANISOU 1849 CD ARG A 242 3474 3625 3667 213 44 79 C
ATOM 1850 NE ARG A 242 15.560 53.688 66.387 1.00 39.51 N
ANISOU 1850 NE ARG A 242 4903 5034 5074 216 50 71 N
ATOM 1851 CZ ARG A 242 15.015 53.483 67.596 1.00 47.92 C
ANISOU 1851 CZ ARG A 242 5966 6107 6135 227 61 77 C
ATOM 1852 NH1 ARG A 242 15.785 53.534 68.679 1.00 54.43 N
ANISOU 1852 NH1 ARG A 242 6805 6926 6951 228 65 70 N
ATOM 1853 NH2 ARG A 242 13.715 53.213 67.741 1.00 50.79 N
ANISOU 1853 NH2 ARG A 242 6311 6485 6503 235 68 91 N
ATOM 1854 N PRO A 243 19.444 53.090 63.024 1.00 10.54 N
ANISOU 1854 N PRO A 243 1256 1336 1414 158 12 38 N
ATOM 1855 CA PRO A 243 20.464 52.298 63.720 1.00 10.55 C
ANISOU 1855 CA PRO A 243 1261 1334 1415 149 11 31 C
ATOM 1856 C PRO A 243 19.978 51.805 65.056 1.00 10.20 C
ANISOU 1856 C PRO A 243 1212 1295 1369 157 19 37 C
ATOM 1857 O PRO A 243 19.294 52.535 65.769 1.00 10.58 O
ANISOU 1857 O PRO A 243 1264 1345 1411 172 27 41 O
ATOM 1858 CB PRO A 243 21.628 53.260 63.922 1.00 11.77 C
ANISOU 1858 CB PRO A 243 1435 1476 1562 148 9 20 C
ATOM 1859 CG PRO A 243 21.106 54.627 63.627 1.00 13.21 C
ANISOU 1859 CG PRO A 243 1627 1655 1740 160 12 22 C
ATOM 1860 CD PRO A 243 19.856 54.488 62.790 1.00 12.11 C
ANISOU 1860 CD PRO A 243 1471 1523 1606 165 12 33 C
ATOM 1861 N ILE A 244 20.301 50.552 65.385 1.00 9.48 N
ANISOU 1861 N ILE A 244 1112 1206 1283 147 17 39 N
ATOM 1862 CA ILE A 244 19.819 49.963 66.638 1.00 9.68 C
ANISOU 1862 CA ILE A 244 1133 1239 1308 154 25 46 C
ATOM 1863 C ILE A 244 20.493 50.583 67.892 1.00 9.49 C
ANISOU 1863 C ILE A 244 1124 1211 1271 162 29 41 C
ATOM 1864 O ILE A 244 19.847 50.726 68.952 1.00 9.68 O
ANISOU 1864 O ILE A 244 1148 1241 1288 174 38 47 O
ATOM 1865 CB ILE A 244 19.855 48.433 66.628 1.00 10.26 C
ANISOU 1865 CB ILE A 244 1192 1314 1390 142 23 51 C
ATOM 1866 CG1 ILE A 244 19.352 47.918 67.948 1.00 11.00 C
ANISOU 1866 CG1 ILE A 244 1282 1416 1482 149 32 61 C
ATOM 1867 CG2 ILE A 244 21.234 47.927 66.286 1.00 9.77 C
ANISOU 1867 CG2 ILE A 244 1137 1244 1331 130 15 42 C
ATOM 1868 CD1 ILE A 244 19.142 46.451 67.957 1.00 11.55 C
ANISOU 1868 CD1 ILE A 244 1338 1487 1563 139 31 69 C
ATOM 1869 N PHE A 245 21.792 50.860 67.788 1.00 9.20 N
ANISOU 1869 N PHE A 245 1100 1166 1230 155 23 30 N
ATOM 1870 CA PHE A 245 22.599 51.316 68.932 1.00 9.26 C
ANISOU 1870 CA PHE A 245 1122 1171 1226 159 25 23 C
ATOM 1871 C PHE A 245 23.375 52.618 68.555 1.00 9.41 C
ANISOU 1871 C PHE A 245 1158 1180 1238 158 20 11 C
ATOM 1872 O PHE A 245 24.589 52.590 68.288 1.00 9.21 O
ANISOU 1872 O PHE A 245 1138 1150 1212 146 13 2 O
ATOM 1873 CB PHE A 245 23.615 50.275 69.338 1.00 9.40 C
ANISOU 1873 CB PHE A 245 1137 1191 1245 149 20 22 C
ATOM 1874 CG PHE A 245 23.040 48.914 69.685 1.00 9.65 C
ANISOU 1874 CG PHE A 245 1154 1229 1285 148 23 34 C
ATOM 1875 CD1 PHE A 245 22.104 48.747 70.694 1.00 10.62 C
ANISOU 1875 CD1 PHE A 245 1272 1360 1403 159 33 44 C
ATOM 1876 CD2 PHE A 245 23.444 47.778 68.963 1.00 9.38 C
ANISOU 1876 CD2 PHE A 245 1109 1192 1262 136 18 35 C
ATOM 1877 CE1 PHE A 245 21.629 47.455 70.966 1.00 10.40 C
ANISOU 1877 CE1 PHE A 245 1231 1338 1384 156 36 56 C
ATOM 1878 CE2 PHE A 245 22.925 46.515 69.218 1.00 10.54 C
ANISOU 1878 CE2 PHE A 245 1244 1343 1418 133 21 46 C
ATOM 1879 CZ PHE A 245 22.058 46.369 70.235 1.00 10.59 C
ANISOU 1879 CZ PHE A 245 1246 1357 1420 143 30 56 C
ATOM 1880 N PRO A 246 22.669 53.757 68.466 1.00 10.49 N
ANISOU 1880 N PRO A 246 1302 1313 1370 169 26 10 N
ATOM 1881 CA PRO A 246 23.318 54.991 68.035 1.00 11.27 C
ANISOU 1881 CA PRO A 246 1417 1400 1464 167 22 0 C
ATOM 1882 C PRO A 246 24.025 55.741 69.193 1.00 11.57 C
ANISOU 1882 C PRO A 246 1475 1433 1489 170 24 -10 C
ATOM 1883 O PRO A 246 23.630 56.876 69.556 1.00 12.46 O
ANISOU 1883 O PRO A 246 1601 1539 1593 181 30 -14 O
ATOM 1884 CB PRO A 246 22.146 55.780 67.476 1.00 11.44 C
ANISOU 1884 CB PRO A 246 1439 1420 1488 180 28 6 C
ATOM 1885 CG PRO A 246 21.029 55.391 68.298 1.00 12.02 C
ANISOU 1885 CG PRO A 246 1503 1503 1560 193 37 16 C
ATOM 1886 CD PRO A 246 21.210 53.910 68.573 1.00 11.74 C
ANISOU 1886 CD PRO A 246 1453 1478 1530 183 35 21 C
ATOM 1887 N GLY A 247 25.090 55.180 69.752 1.00 11.20 N
ANISOU 1887 N GLY A 247 1429 1389 1438 160 19 -15 N
ATOM 1888 CA GLY A 247 25.793 55.847 70.873 1.00 12.94 C
ANISOU 1888 CA GLY A 247 1666 1607 1644 161 19 -25 C
ATOM 1889 C GLY A 247 26.311 57.207 70.441 1.00 14.30 C
ANISOU 1889 C GLY A 247 1857 1765 1813 158 16 -37 C
ATOM 1890 O GLY A 247 26.827 57.365 69.316 1.00 14.40 O
ANISOU 1890 O GLY A 247 1867 1771 1832 147 10 -39 O
ATOM 1891 N LYS A 248 26.256 58.166 71.364 1.00 15.48 N
ANISOU 1891 N LYS A 248 2024 1909 1950 165 21 -45 N
ATOM 1892 CA LYS A 248 26.668 59.553 71.126 1.00 18.09 C
ANISOU 1892 CA LYS A 248 2374 2223 2275 163 21 -56 C
ATOM 1893 C LYS A 248 28.105 59.807 71.499 1.00 18.05 C
ANISOU 1893 C LYS A 248 2380 2216 2263 146 11 -69 C
ATOM 1894 O LYS A 248 28.632 60.874 71.206 1.00 18.67 O
ANISOU 1894 O LYS A 248 2474 2280 2339 139 9 -78 O
ATOM 1895 CB LYS A 248 25.798 60.473 71.956 1.00 19.69 C
ANISOU 1895 CB LYS A 248 2592 2420 2468 181 32 -59 C
ATOM 1896 CG LYS A 248 24.326 60.439 71.627 1.00 23.00 C
ANISOU 1896 CG LYS A 248 3003 2843 2894 199 42 -47 C
ATOM 1897 CD LYS A 248 23.518 61.508 72.358 1.00 27.60 C
ANISOU 1897 CD LYS A 248 3602 3417 3466 219 54 -51 C
ATOM 1898 CE LYS A 248 22.073 61.429 71.852 1.00 31.68 C
ANISOU 1898 CE LYS A 248 4105 3939 3992 237 64 -36 C
ATOM 1899 NZ LYS A 248 21.127 62.431 72.401 1.00 36.16 N
ANISOU 1899 NZ LYS A 248 4686 4499 4552 259 77 -37 N
ATOM 1900 N HIS A 249 28.737 58.841 72.145 1.00 17.09 N
ANISOU 1900 N HIS A 249 2248 2107 2138 140 6 -68 N
ATOM 1901 CA HIS A 249 30.127 58.878 72.511 1.00 16.23 C
ANISOU 1901 CA HIS A 249 2143 2000 2022 124 -4 -78 C
ATOM 1902 C HIS A 249 30.510 57.480 72.912 1.00 15.52 C
ANISOU 1902 C HIS A 249 2036 1926 1933 121 -8 -70 C
ATOM 1903 O HIS A 249 29.668 56.569 72.942 1.00 15.38 O
ANISOU 1903 O HIS A 249 2005 1917 1922 131 -3 -58 O
ATOM 1904 CB HIS A 249 30.399 59.900 73.659 1.00 16.57 C
ANISOU 1904 CB HIS A 249 2209 2038 2048 125 -3 -91 C
ATOM 1905 CG HIS A 249 29.553 59.714 74.885 1.00 16.98 C
ANISOU 1905 CG HIS A 249 2264 2099 2089 141 6 -89 C
ATOM 1906 ND1 HIS A 249 29.850 58.804 75.878 1.00 19.36 N
ANISOU 1906 ND1 HIS A 249 2558 2417 2382 142 3 -86 N
ATOM 1907 CD2 HIS A 249 28.471 60.397 75.314 1.00 18.66 C
ANISOU 1907 CD2 HIS A 249 2489 2305 2295 159 18 -90 C
ATOM 1908 CE1 HIS A 249 28.982 58.940 76.867 1.00 19.52 C
ANISOU 1908 CE1 HIS A 249 2585 2442 2391 158 13 -85 C
ATOM 1909 NE2 HIS A 249 28.111 59.868 76.529 1.00 19.47 N
ANISOU 1909 NE2 HIS A 249 2590 2422 2387 169 22 -87 N
ATOM 1910 N TYR A 250 31.780 57.282 73.164 1.00 15.95 N
ANISOU 1910 N TYR A 250 2089 1986 1984 107 -18 -76 N
ATOM 1911 CA TYR A 250 32.383 55.958 73.312 1.00 13.89 C
ANISOU 1911 CA TYR A 250 1811 1739 1728 102 -24 -68 C
ATOM 1912 C TYR A 250 31.672 55.040 74.334 1.00 14.51 C
ANISOU 1912 C TYR A 250 1882 1830 1801 116 -18 -58 C
ATOM 1913 O TYR A 250 31.234 53.934 74.028 1.00 14.97 O
ANISOU 1913 O TYR A 250 1925 1893 1870 120 -15 -46 O
ATOM 1914 CB TYR A 250 33.858 56.127 73.672 1.00 14.49 C
ANISOU 1914 CB TYR A 250 1889 1820 1795 87 -35 -77 C
ATOM 1915 CG TYR A 250 34.573 54.831 73.777 1.00 13.46 C
ANISOU 1915 CG TYR A 250 1741 1704 1670 84 -41 -69 C
ATOM 1916 CD1 TYR A 250 34.435 54.047 74.906 1.00 14.16 C
ANISOU 1916 CD1 TYR A 250 1824 1805 1750 92 -40 -62 C
ATOM 1917 CD2 TYR A 250 35.377 54.386 72.755 1.00 13.29 C
ANISOU 1917 CD2 TYR A 250 1707 1682 1660 73 -47 -67 C
ATOM 1918 CE1 TYR A 250 35.113 52.856 75.013 1.00 14.21 C
ANISOU 1918 CE1 TYR A 250 1815 1823 1761 90 -45 -53 C
ATOM 1919 CE2 TYR A 250 36.045 53.167 72.827 1.00 13.65 C
ANISOU 1919 CE2 TYR A 250 1737 1740 1712 72 -51 -59 C
ATOM 1920 CZ TYR A 250 35.899 52.394 73.960 1.00 13.49 C
ANISOU 1920 CZ TYR A 250 1712 1730 1684 81 -50 -52 C
ATOM 1921 OH TYR A 250 36.550 51.220 74.047 1.00 14.29 O
ANISOU 1921 OH TYR A 250 1798 1841 1790 80 -54 -43 O
ATOM 1922 N LEU A 251 31.504 55.509 75.567 1.00 14.65 N
ANISOU 1922 N LEU A 251 1912 1852 1802 122 -15 -63 N
ATOM 1923 CA LEU A 251 30.888 54.694 76.603 1.00 13.96 C
ANISOU 1923 CA LEU A 251 1819 1777 1708 135 -9 -53 C
ATOM 1924 C LEU A 251 29.354 54.555 76.409 1.00 13.06 C
ANISOU 1924 C LEU A 251 1701 1661 1601 150 4 -43 C
ATOM 1925 O LEU A 251 28.743 53.521 76.737 1.00 13.05 O
ANISOU 1925 O LEU A 251 1687 1669 1604 157 9 -30 O
ATOM 1926 CB LEU A 251 31.193 55.358 77.978 1.00 15.38 C
ANISOU 1926 CB LEU A 251 2015 1964 1866 137 -10 -63 C
ATOM 1927 CG LEU A 251 30.633 54.620 79.171 1.00 16.56 C
ANISOU 1927 CG LEU A 251 2161 2128 2005 149 -4 -53 C
ATOM 1928 CD1 LEU A 251 31.201 53.222 79.282 1.00 17.39 C
ANISOU 1928 CD1 LEU A 251 2246 2245 2115 146 -10 -40 C
ATOM 1929 CD2 LEU A 251 30.883 55.441 80.434 1.00 18.19 C
ANISOU 1929 CD2 LEU A 251 2385 2339 2187 152 -4 -65 C
ATOM 1930 N ASP A 252 28.754 55.623 75.882 1.00 12.12 N
ANISOU 1930 N ASP A 252 1592 1529 1483 154 9 -49 N
ATOM 1931 CA ASP A 252 27.342 55.613 75.538 1.00 11.65 C
ANISOU 1931 CA ASP A 252 1528 1467 1431 168 20 -40 C
ATOM 1932 C ASP A 252 27.025 54.451 74.617 1.00 11.32 C
ANISOU 1932 C ASP A 252 1465 1430 1407 164 19 -27 C
ATOM 1933 O ASP A 252 25.936 53.901 74.691 1.00 10.97 O
ANISOU 1933 O ASP A 252 1410 1390 1368 174 27 -15 O
ATOM 1934 CB ASP A 252 26.942 56.916 74.839 1.00 12.42 C
ANISOU 1934 CB ASP A 252 1639 1550 1531 171 23 -48 C
ATOM 1935 CG ASP A 252 25.439 57.146 74.822 1.00 12.37 C
ANISOU 1935 CG ASP A 252 1630 1543 1527 190 36 -40 C
ATOM 1936 OD1 ASP A 252 24.740 56.867 75.838 1.00 14.41 O
ANISOU 1936 OD1 ASP A 252 1887 1811 1776 202 45 -34 O
ATOM 1937 OD2 ASP A 252 24.916 57.598 73.750 1.00 14.95 O
ANISOU 1937 OD2 ASP A 252 1955 1861 1864 192 38 -37 O
ATOM 1938 N GLN A 253 27.966 54.087 73.734 1.00 10.59 N
ANISOU 1938 N GLN A 253 1366 1333 1324 150 9 -29 N
ATOM 1939 CA GLN A 253 27.719 52.937 72.829 1.00 10.33 C
ANISOU 1939 CA GLN A 253 1315 1303 1308 146 8 -19 C
ATOM 1940 C GLN A 253 27.505 51.666 73.627 1.00 10.10 C
ANISOU 1940 C GLN A 253 1273 1285 1279 150 10 -7 C
ATOM 1941 O GLN A 253 26.574 50.944 73.346 1.00 9.69 O
ANISOU 1941 O GLN A 253 1210 1236 1237 154 16 4 O
ATOM 1942 CB GLN A 253 28.889 52.794 71.892 1.00 10.16 C
ANISOU 1942 CB GLN A 253 1291 1277 1294 131 -3 -24 C
ATOM 1943 CG GLN A 253 28.669 51.734 70.810 1.00 9.57 C
ANISOU 1943 CG GLN A 253 1199 1202 1235 126 -4 -16 C
ATOM 1944 CD GLN A 253 27.556 52.163 69.898 1.00 9.43 C
ANISOU 1944 CD GLN A 253 1180 1179 1225 130 1 -13 C
ATOM 1945 OE1 GLN A 253 27.382 53.351 69.624 1.00 10.48 O
ANISOU 1945 OE1 GLN A 253 1324 1304 1353 133 2 -19 O
ATOM 1946 NE2 GLN A 253 26.768 51.198 69.438 1.00 8.86 N
ANISOU 1946 NE2 GLN A 253 1093 1110 1163 132 4 -3 N
ATOM 1947 N LEU A 254 28.374 51.382 74.586 1.00 11.26 N
ANISOU 1947 N LEU A 254 1423 1439 1416 147 6 -9 N
ATOM 1948 CA LEU A 254 28.172 50.211 75.457 1.00 11.08 C
ANISOU 1948 CA LEU A 254 1390 1427 1392 152 9 4 C
ATOM 1949 C LEU A 254 26.855 50.294 76.197 1.00 11.10 C
ANISOU 1949 C LEU A 254 1394 1436 1389 167 22 12 C
ATOM 1950 O LEU A 254 26.127 49.314 76.287 1.00 11.28 O
ANISOU 1950 O LEU A 254 1404 1463 1420 170 27 26 O
ATOM 1951 CB LEU A 254 29.340 50.129 76.415 1.00 11.98 C
ANISOU 1951 CB LEU A 254 1509 1549 1492 149 2 0 C
ATOM 1952 CG LEU A 254 29.250 49.003 77.474 1.00 12.18 C
ANISOU 1952 CG LEU A 254 1527 1586 1513 155 5 14 C
ATOM 1953 CD1 LEU A 254 29.241 47.630 76.762 1.00 12.50 C
ANISOU 1953 CD1 LEU A 254 1551 1625 1574 151 5 26 C
ATOM 1954 CD2 LEU A 254 30.375 49.114 78.488 1.00 12.46 C
ANISOU 1954 CD2 LEU A 254 1569 1632 1533 153 -2 9 C
ATOM 1955 N ASN A 255 26.504 51.465 76.684 1.00 11.57 N
ANISOU 1955 N ASN A 255 1468 1493 1435 174 26 4 N
ATOM 1956 CA ASN A 255 25.278 51.617 77.442 1.00 11.90 C
ANISOU 1956 CA ASN A 255 1511 1542 1470 190 39 11 C
ATOM 1957 C ASN A 255 24.024 51.365 76.578 1.00 11.55 C
ANISOU 1957 C ASN A 255 1453 1494 1441 194 46 21 C
ATOM 1958 O ASN A 255 23.041 50.758 77.009 1.00 10.98 O
ANISOU 1958 O ASN A 255 1370 1431 1370 202 56 34 O
ATOM 1959 CB ASN A 255 25.239 52.986 78.111 1.00 12.32 C
ANISOU 1959 CB ASN A 255 1584 1592 1506 198 43 -3 C
ATOM 1960 CG ASN A 255 26.271 53.121 79.223 1.00 13.12 C
ANISOU 1960 CG ASN A 255 1696 1700 1588 194 37 -11 C
ATOM 1961 OD1 ASN A 255 26.751 52.097 79.784 1.00 13.93 O
ANISOU 1961 OD1 ASN A 255 1790 1813 1689 191 33 -2 O
ATOM 1962 ND2 ASN A 255 26.623 54.326 79.550 1.00 14.03 N
ANISOU 1962 ND2 ASN A 255 1831 1809 1691 194 36 -26 N
ATOM 1963 N HIS A 256 24.069 51.828 75.323 1.00 10.79 N
ANISOU 1963 N HIS A 256 1357 1388 1356 188 42 15 N
ATOM 1964 CA HIS A 256 23.017 51.516 74.366 1.00 10.62 C
ANISOU 1964 CA HIS A 256 1321 1364 1348 190 45 24 C
ATOM 1965 C HIS A 256 22.804 50.009 74.229 1.00 10.19 C
ANISOU 1965 C HIS A 256 1248 1316 1306 183 45 38 C
ATOM 1966 O HIS A 256 21.683 49.496 74.207 1.00 10.76 O
ANISOU 1966 O HIS A 256 1308 1395 1385 188 52 50 O
ATOM 1967 CB HIS A 256 23.313 52.142 72.992 1.00 11.14 C
ANISOU 1967 CB HIS A 256 1390 1419 1424 182 38 16 C
ATOM 1968 CG HIS A 256 22.764 53.527 72.858 1.00 11.80 C
ANISOU 1968 CG HIS A 256 1486 1496 1501 193 44 10 C
ATOM 1969 ND1 HIS A 256 21.603 53.763 72.167 1.00 14.08 N
ANISOU 1969 ND1 HIS A 256 1766 1785 1798 200 49 18 N
ATOM 1970 CD2 HIS A 256 23.153 54.718 73.377 1.00 12.38 C
ANISOU 1970 CD2 HIS A 256 1579 1563 1562 197 45 -2 C
ATOM 1971 CE1 HIS A 256 21.322 55.051 72.229 1.00 14.49 C
ANISOU 1971 CE1 HIS A 256 1833 1830 1842 211 54 11 C
ATOM 1972 NE2 HIS A 256 22.272 55.653 72.914 1.00 13.77 N
ANISOU 1972 NE2 HIS A 256 1760 1734 1740 209 51 -1 N
ATOM 1973 N ILE A 257 23.932 49.302 74.088 1.00 9.63 N
ANISOU 1973 N ILE A 257 1175 1243 1239 172 36 35 N
ATOM 1974 CA ILE A 257 23.885 47.854 73.860 1.00 9.66 C
ANISOU 1974 CA ILE A 257 1165 1250 1257 165 35 46 C
ATOM 1975 C ILE A 257 23.260 47.173 75.051 1.00 10.71 C
ANISOU 1975 C ILE A 257 1292 1392 1384 173 44 60 C
ATOM 1976 O ILE A 257 22.365 46.318 74.894 1.00 9.67 O
ANISOU 1976 O ILE A 257 1147 1264 1264 172 49 72 O
ATOM 1977 CB ILE A 257 25.265 47.306 73.548 1.00 9.91 C
ANISOU 1977 CB ILE A 257 1197 1277 1292 153 24 41 C
ATOM 1978 CG1 ILE A 257 25.750 47.850 72.172 1.00 9.68 C
ANISOU 1978 CG1 ILE A 257 1170 1238 1270 144 17 30 C
ATOM 1979 CG2 ILE A 257 25.226 45.786 73.516 1.00 10.15 C
ANISOU 1979 CG2 ILE A 257 1214 1308 1335 148 25 53 C
ATOM 1980 CD1 ILE A 257 27.212 47.665 71.893 1.00 10.05 C
ANISOU 1980 CD1 ILE A 257 1219 1281 1317 134 7 22 C
ATOM 1981 N LEU A 258 23.728 47.571 76.245 1.00 10.72 N
ANISOU 1981 N LEU A 258 1304 1401 1369 180 45 57 N
ATOM 1982 CA LEU A 258 23.281 46.957 77.494 1.00 11.77 C
ANISOU 1982 CA LEU A 258 1433 1544 1493 188 54 70 C
ATOM 1983 C LEU A 258 21.809 47.284 77.778 1.00 12.01 C
ANISOU 1983 C LEU A 258 1459 1581 1521 199 67 78 C
ATOM 1984 O LEU A 258 21.103 46.514 78.378 1.00 12.42 O
ANISOU 1984 O LEU A 258 1502 1642 1575 203 75 92 O
ATOM 1985 CB LEU A 258 24.178 47.394 78.625 1.00 12.46 C
ANISOU 1985 CB LEU A 258 1535 1639 1561 192 51 63 C
ATOM 1986 CG LEU A 258 25.600 46.832 78.573 1.00 13.78 C
ANISOU 1986 CG LEU A 258 1703 1804 1730 181 39 60 C
ATOM 1987 CD1 LEU A 258 26.384 47.476 79.683 1.00 15.06 C
ANISOU 1987 CD1 LEU A 258 1879 1974 1870 185 36 52 C
ATOM 1988 CD2 LEU A 258 25.652 45.316 78.648 1.00 15.16 C
ANISOU 1988 CD2 LEU A 258 1863 1980 1916 178 39 76 C
ATOM 1989 N GLY A 259 21.346 48.420 77.272 1.00 11.83 N
ANISOU 1989 N GLY A 259 1443 1555 1498 205 69 69 N
ATOM 1990 CA GLY A 259 19.921 48.795 77.412 1.00 12.57 C
ANISOU 1990 CA GLY A 259 1530 1654 1590 217 81 76 C
ATOM 1991 C GLY A 259 18.956 47.850 76.701 1.00 12.65 C
ANISOU 1991 C GLY A 259 1520 1667 1619 212 84 91 C
ATOM 1992 O GLY A 259 17.758 47.684 77.116 1.00 13.17 O
ANISOU 1992 O GLY A 259 1575 1743 1685 221 96 103 O
ATOM 1993 N ILE A 260 19.434 47.189 75.649 1.00 11.53 N
ANISOU 1993 N ILE A 260 1371 1517 1492 197 74 89 N
ATOM 1994 CA ILE A 260 18.618 46.237 74.944 1.00 11.69 C
ANISOU 1994 CA ILE A 260 1373 1539 1530 189 75 101 C
ATOM 1995 C ILE A 260 18.924 44.801 75.312 1.00 11.30 C
ANISOU 1995 C ILE A 260 1316 1489 1488 180 74 111 C
ATOM 1996 O ILE A 260 18.023 44.040 75.633 1.00 10.94 O
ANISOU 1996 O ILE A 260 1258 1451 1449 180 82 126 O
ATOM 1997 CB ILE A 260 18.715 46.460 73.415 1.00 12.20 C
ANISOU 1997 CB ILE A 260 1435 1594 1607 180 65 93 C
ATOM 1998 CG1 ILE A 260 17.928 47.723 73.026 1.00 13.47 C
ANISOU 1998 CG1 ILE A 260 1598 1757 1764 191 69 89 C
ATOM 1999 CG2 ILE A 260 18.238 45.218 72.672 1.00 12.18 C
ANISOU 1999 CG2 ILE A 260 1415 1590 1621 166 63 102 C
ATOM 2000 CD1 ILE A 260 18.145 48.263 71.623 1.00 14.13 C
ANISOU 2000 CD1 ILE A 260 1683 1832 1854 184 60 80 C
ATOM 2001 N LEU A 261 20.195 44.460 75.412 1.00 10.87 N
ANISOU 2001 N LEU A 261 1270 1429 1433 174 66 105 N
ATOM 2002 CA LEU A 261 20.572 43.110 75.757 1.00 11.48 C
ANISOU 2002 CA LEU A 261 1341 1505 1517 167 65 115 C
ATOM 2003 C LEU A 261 20.365 42.769 77.211 1.00 11.39 C
ANISOU 2003 C LEU A 261 1330 1504 1494 176 75 128 C
ATOM 2004 O LEU A 261 20.260 41.572 77.547 1.00 11.24 O
ANISOU 2004 O LEU A 261 1303 1485 1483 172 78 142 O
ATOM 2005 CB LEU A 261 22.011 42.838 75.399 1.00 11.65 C
ANISOU 2005 CB LEU A 261 1369 1517 1540 159 54 106 C
ATOM 2006 CG LEU A 261 22.373 42.780 73.931 1.00 12.62 C
ANISOU 2006 CG LEU A 261 1490 1629 1677 148 45 96 C
ATOM 2007 CD1 LEU A 261 23.798 42.249 73.781 1.00 12.75 C
ANISOU 2007 CD1 LEU A 261 1511 1638 1696 141 37 90 C
ATOM 2008 CD2 LEU A 261 21.367 42.021 73.146 1.00 14.45 C
ANISOU 2008 CD2 LEU A 261 1707 1857 1925 140 48 103 C
ATOM 2009 N GLY A 262 20.327 43.805 78.040 1.00 11.20 N
ANISOU 2009 N GLY A 262 1316 1487 1450 189 79 123 N
ATOM 2010 CA GLY A 262 20.179 43.651 79.497 1.00 11.79 C
ANISOU 2010 CA GLY A 262 1395 1576 1511 199 88 133 C
ATOM 2011 C GLY A 262 21.499 43.341 80.168 1.00 11.26 C
ANISOU 2011 C GLY A 262 1336 1508 1433 198 81 131 C
ATOM 2012 O GLY A 262 22.558 43.314 79.538 1.00 11.54 O
ANISOU 2012 O GLY A 262 1377 1535 1474 189 69 121 O
ATOM 2013 N SER A 263 21.438 43.111 81.482 1.00 11.13 N
ANISOU 2013 N SER A 263 1323 1504 1402 206 88 141 N
ATOM 2014 CA SER A 263 22.626 42.802 82.279 1.00 11.07 C
ANISOU 2014 CA SER A 263 1323 1500 1382 207 81 141 C
ATOM 2015 C SER A 263 23.256 41.492 81.832 1.00 11.46 C
ANISOU 2015 C SER A 263 1364 1541 1449 196 75 150 C
ATOM 2016 O SER A 263 22.581 40.452 81.714 1.00 12.50 O
ANISOU 2016 O SER A 263 1484 1670 1596 193 81 166 O
ATOM 2017 CB SER A 263 22.207 42.656 83.741 1.00 11.71 C
ANISOU 2017 CB SER A 263 1406 1597 1444 218 92 154 C
ATOM 2018 OG SER A 263 21.564 43.831 84.151 1.00 12.43 O
ANISOU 2018 OG SER A 263 1506 1696 1520 229 99 145 O
ATOM 2019 N PRO A 264 24.569 41.480 81.643 1.00 11.82 N
ANISOU 2019 N PRO A 264 1415 1582 1493 192 63 141 N
ATOM 2020 CA PRO A 264 25.213 40.197 81.366 1.00 11.90 C
ANISOU 2020 CA PRO A 264 1418 1585 1518 185 58 151 C
ATOM 2021 C PRO A 264 24.990 39.192 82.471 1.00 12.29 C
ANISOU 2021 C PRO A 264 1463 1642 1564 191 65 173 C
ATOM 2022 O PRO A 264 25.008 39.553 83.636 1.00 13.07 O
ANISOU 2022 O PRO A 264 1568 1756 1642 200 69 177 O
ATOM 2023 CB PRO A 264 26.710 40.583 81.207 1.00 11.85 C
ANISOU 2023 CB PRO A 264 1419 1578 1506 182 44 138 C
ATOM 2024 CG PRO A 264 26.666 41.997 80.724 1.00 12.22 C
ANISOU 2024 CG PRO A 264 1474 1623 1545 181 41 118 C
ATOM 2025 CD PRO A 264 25.475 42.604 81.423 1.00 12.44 C
ANISOU 2025 CD PRO A 264 1505 1660 1561 190 53 121 C
ATOM 2026 N SER A 265 24.821 37.939 82.072 1.00 12.55 N
ANISOU 2026 N SER A 265 1486 1665 1617 185 68 186 N
ATOM 2027 CA SER A 265 24.731 36.847 83.002 1.00 13.17 C
ANISOU 2027 CA SER A 265 1561 1748 1696 189 74 209 C
ATOM 2028 C SER A 265 26.000 36.696 83.798 1.00 13.39 C
ANISOU 2028 C SER A 265 1596 1784 1710 195 67 211 C
ATOM 2029 O SER A 265 27.082 37.117 83.363 1.00 13.17 O
ANISOU 2029 O SER A 265 1571 1753 1679 192 55 197 O
ATOM 2030 CB SER A 265 24.453 35.545 82.262 1.00 12.83 C
ANISOU 2030 CB SER A 265 1509 1688 1679 179 77 220 C
ATOM 2031 OG SER A 265 25.558 35.120 81.455 1.00 13.43 O
ANISOU 2031 OG SER A 265 1585 1750 1766 174 66 211 O
ATOM 2032 N GLN A 266 25.912 35.942 84.904 1.00 13.94 N
ANISOU 2032 N GLN A 266 1663 1861 1771 202 73 232 N
ATOM 2033 CA GLN A 266 27.117 35.614 85.684 1.00 15.27 C
ANISOU 2033 CA GLN A 266 1836 2039 1928 208 65 238 C
ATOM 2034 C GLN A 266 28.178 34.876 84.874 1.00 13.72 C
ANISOU 2034 C GLN A 266 1635 1827 1749 203 56 237 C
ATOM 2035 O GLN A 266 29.394 35.165 84.994 1.00 13.04 O
ANISOU 2035 O GLN A 266 1553 1748 1654 205 44 229 O
ATOM 2036 CB GLN A 266 26.744 34.832 86.943 1.00 16.84 C
ANISOU 2036 CB GLN A 266 2033 2249 2118 216 75 264 C
ATOM 2037 CG GLN A 266 27.889 34.707 87.936 1.00 18.62 C
ANISOU 2037 CG GLN A 266 2263 2489 2324 225 67 271 C
ATOM 2038 CD GLN A 266 28.328 36.061 88.455 1.00 19.76 C
ANISOU 2038 CD GLN A 266 2417 2650 2440 229 59 252 C
ATOM 2039 OE1 GLN A 266 27.540 36.793 89.042 1.00 22.10 O
ANISOU 2039 OE1 GLN A 266 2718 2958 2720 233 67 249 O
ATOM 2040 NE2 GLN A 266 29.604 36.444 88.170 1.00 20.85 N
ANISOU 2040 NE2 GLN A 266 2558 2790 2574 227 44 238 N
ATOM 2041 N GLU A 267 27.778 33.927 84.028 1.00 12.39 N
ANISOU 2041 N GLU A 267 1461 1641 1607 196 60 243 N
ATOM 2042 CA GLU A 267 28.743 33.203 83.202 1.00 13.59 C
ANISOU 2042 CA GLU A 267 1611 1777 1777 192 53 240 C
ATOM 2043 C GLU A 267 29.454 34.164 82.263 1.00 12.99 C
ANISOU 2043 C GLU A 267 1536 1699 1699 187 42 215 C
ATOM 2044 O GLU A 267 30.651 34.080 82.092 1.00 12.81 O
ANISOU 2044 O GLU A 267 1514 1676 1677 188 32 210 O
ATOM 2045 CB GLU A 267 28.075 32.070 82.393 1.00 15.42 C
ANISOU 2045 CB GLU A 267 1836 1987 2036 183 60 248 C
ATOM 2046 CG GLU A 267 29.013 31.401 81.418 1.00 17.95 C
ANISOU 2046 CG GLU A 267 2155 2290 2375 180 53 242 C
ATOM 2047 CD GLU A 267 28.351 30.255 80.692 1.00 22.96 C
ANISOU 2047 CD GLU A 267 2785 2902 3035 171 61 250 C
ATOM 2048 OE1 GLU A 267 28.174 29.193 81.311 1.00 30.04 O
ANISOU 2048 OE1 GLU A 267 3682 3794 3940 174 68 271 O
ATOM 2049 OE2 GLU A 267 28.109 30.384 79.496 1.00 26.78 O
ANISOU 2049 OE2 GLU A 267 3268 3374 3532 161 59 234 O
ATOM 2050 N ASP A 268 28.716 35.100 81.678 1.00 12.65 N
ANISOU 2050 N ASP A 268 1496 1656 1656 181 43 200 N
ATOM 2051 CA ASP A 268 29.320 36.056 80.760 1.00 12.44 C
ANISOU 2051 CA ASP A 268 1473 1627 1629 175 33 177 C
ATOM 2052 C ASP A 268 30.220 37.002 81.508 1.00 12.17 C
ANISOU 2052 C ASP A 268 1444 1608 1571 181 25 169 C
ATOM 2053 O ASP A 268 31.331 37.319 80.997 1.00 12.36 O
ANISOU 2053 O ASP A 268 1469 1631 1595 177 15 157 O
ATOM 2054 CB ASP A 268 28.239 36.799 79.923 1.00 12.51 C
ANISOU 2054 CB ASP A 268 1482 1630 1643 169 37 165 C
ATOM 2055 CG ASP A 268 27.608 35.884 78.832 1.00 12.86 C
ANISOU 2055 CG ASP A 268 1518 1656 1712 159 41 168 C
ATOM 2056 OD1 ASP A 268 28.023 34.696 78.605 1.00 14.63 O
ANISOU 2056 OD1 ASP A 268 1738 1869 1951 157 42 177 O
ATOM 2057 OD2 ASP A 268 26.662 36.388 78.150 1.00 14.87 O
ANISOU 2057 OD2 ASP A 268 1771 1908 1972 154 44 161 O
ATOM 2058 N LEU A 269 29.831 37.417 82.712 1.00 11.84 N
ANISOU 2058 N LEU A 269 1408 1583 1509 188 29 175 N
ATOM 2059 CA LEU A 269 30.702 38.244 83.546 1.00 12.94 C
ANISOU 2059 CA LEU A 269 1555 1739 1624 193 21 168 C
ATOM 2060 C LEU A 269 31.987 37.512 83.917 1.00 12.96 C
ANISOU 2060 C LEU A 269 1553 1746 1625 196 12 177 C
ATOM 2061 O LEU A 269 33.071 38.118 83.968 1.00 12.99 O
ANISOU 2061 O LEU A 269 1560 1759 1619 194 0 165 O
ATOM 2062 CB LEU A 269 30.014 38.676 84.815 1.00 13.09 C
ANISOU 2062 CB LEU A 269 1580 1774 1621 201 28 174 C
ATOM 2063 CG LEU A 269 28.864 39.679 84.687 1.00 14.16 C
ANISOU 2063 CG LEU A 269 1721 1910 1751 201 36 164 C
ATOM 2064 CD1 LEU A 269 28.160 39.871 86.049 1.00 14.60 C
ANISOU 2064 CD1 LEU A 269 1781 1982 1784 212 45 174 C
ATOM 2065 CD2 LEU A 269 29.393 40.984 84.120 1.00 13.75 C
ANISOU 2065 CD2 LEU A 269 1676 1855 1691 196 27 139 C
ATOM 2066 N ASN A 270 31.887 36.205 84.175 1.00 12.64 N
ANISOU 2066 N ASN A 270 1506 1701 1597 201 17 198 N
ATOM 2067 CA ASN A 270 33.073 35.419 84.530 1.00 13.36 C
ANISOU 2067 CA ASN A 270 1593 1796 1688 206 10 209 C
ATOM 2068 C ASN A 270 34.047 35.221 83.407 1.00 13.83 C
ANISOU 2068 C ASN A 270 1647 1844 1764 201 2 198 C
ATOM 2069 O ASN A 270 35.163 34.766 83.665 1.00 15.03 O
ANISOU 2069 O ASN A 270 1795 2003 1915 206 -6 205 O
ATOM 2070 CB ASN A 270 32.632 34.081 85.160 1.00 13.44 C
ANISOU 2070 CB ASN A 270 1599 1803 1706 213 20 236 C
ATOM 2071 CG ASN A 270 32.066 34.240 86.547 1.00 14.13 C
ANISOU 2071 CG ASN A 270 1689 1908 1770 221 25 249 C
ATOM 2072 OD1 ASN A 270 32.256 35.256 87.217 1.00 16.34 O
ANISOU 2072 OD1 ASN A 270 1976 2206 2025 223 20 239 O
ATOM 2073 ND2 ASN A 270 31.361 33.259 86.996 1.00 14.16 N
ANISOU 2073 ND2 ASN A 270 1691 1909 1782 225 36 271 N
ATOM 2074 N CYS A 271 33.687 35.605 82.192 1.00 13.75 N
ANISOU 2074 N CYS A 271 1637 1819 1767 191 3 182 N
ATOM 2075 CA CYS A 271 34.604 35.591 81.037 1.00 13.82 C
ANISOU 2075 CA CYS A 271 1641 1818 1790 185 -4 170 C
ATOM 2076 C CYS A 271 35.312 36.983 80.885 1.00 12.73 C
ANISOU 2076 C CYS A 271 1508 1692 1637 180 -15 149 C
ATOM 2077 O CYS A 271 36.043 37.144 79.935 1.00 13.64 O
ANISOU 2077 O CYS A 271 1620 1801 1761 174 -21 137 O
ATOM 2078 CB CYS A 271 33.827 35.277 79.770 1.00 14.53 C
ANISOU 2078 CB CYS A 271 1731 1888 1903 177 2 163 C
ATOM 2079 SG CYS A 271 33.120 33.600 79.641 1.00 18.54 S
ANISOU 2079 SG CYS A 271 2234 2377 2434 180 14 184 S
ATOM 2080 N ILE A 272 35.057 37.903 81.804 1.00 12.95 N
ANISOU 2080 N ILE A 272 1544 1735 1643 181 -17 145 N
ATOM 2081 CA ILE A 272 35.629 39.285 81.787 1.00 13.44 C
ANISOU 2081 CA ILE A 272 1612 1807 1689 175 -26 126 C
ATOM 2082 C ILE A 272 36.402 39.450 83.069 1.00 12.59 C
ANISOU 2082 C ILE A 272 1506 1720 1558 180 -34 131 C
ATOM 2083 O ILE A 272 35.820 39.564 84.124 1.00 14.79 O
ANISOU 2083 O ILE A 272 1790 2009 1820 186 -30 138 O
ATOM 2084 CB ILE A 272 34.553 40.381 81.630 1.00 13.76 C
ANISOU 2084 CB ILE A 272 1662 1843 1722 171 -20 113 C
ATOM 2085 CG1 ILE A 272 33.779 40.189 80.311 1.00 13.66 C
ANISOU 2085 CG1 ILE A 272 1646 1811 1731 165 -14 108 C
ATOM 2086 CG2 ILE A 272 35.177 41.797 81.594 1.00 14.40 C
ANISOU 2086 CG2 ILE A 272 1751 1931 1788 164 -30 92 C
ATOM 2087 CD1 ILE A 272 32.533 40.999 80.262 1.00 13.78 C
ANISOU 2087 CD1 ILE A 272 1670 1824 1743 165 -6 102 C
ATOM 2088 N ILE A 273 37.722 39.411 82.982 1.00 11.74 N
ANISOU 2088 N ILE A 273 1391 1620 1448 178 -45 128 N
ATOM 2089 CA AILE A 273 38.650 39.473 84.124 0.30 11.37 C
ANISOU 2089 CA AILE A 273 1344 1596 1381 183 -55 134 C
ATOM 2090 CA BILE A 273 38.520 39.539 84.226 0.70 11.44 C
ANISOU 2090 CA BILE A 273 1353 1605 1388 183 -55 134 C
ATOM 2091 C ILE A 273 39.176 40.909 84.400 1.00 11.24 C
ANISOU 2091 C ILE A 273 1334 1592 1343 173 -66 114 C
ATOM 2092 O ILE A 273 39.674 41.222 85.478 1.00 10.79 O
ANISOU 2092 O ILE A 273 1280 1555 1264 175 -74 116 O
ATOM 2093 CB AILE A 273 39.841 38.540 83.817 0.30 11.46 C
ANISOU 2093 CB AILE A 273 1341 1609 1405 186 -62 145 C
ATOM 2094 CB BILE A 273 39.531 38.366 84.434 0.70 11.76 C
ANISOU 2094 CB BILE A 273 1381 1652 1435 191 -60 152 C
ATOM 2095 CG1AILE A 273 39.360 37.101 83.589 0.30 11.49 C
ANISOU 2095 CG1AILE A 273 1338 1598 1429 196 -51 164 C
ATOM 2096 CG1BILE A 273 40.749 38.521 83.531 0.70 12.21 C
ANISOU 2096 CG1BILE A 273 1429 1709 1502 184 -70 142 C
ATOM 2097 CG2AILE A 273 40.889 38.572 84.912 0.30 11.60 C
ANISOU 2097 CG2AILE A 273 1354 1651 1401 191 -74 152 C
ATOM 2098 CG2BILE A 273 38.870 36.979 84.203 0.70 11.96 C
ANISOU 2098 CG2BILE A 273 1401 1661 1481 200 -47 172 C
ATOM 2099 CD1AILE A 273 38.390 36.617 84.642 0.30 11.57 C
ANISOU 2099 CD1AILE A 273 1353 1612 1430 205 -42 182 C
ATOM 2100 CD1BILE A 273 41.838 37.517 83.854 0.70 12.33 C
ANISOU 2100 CD1BILE A 273 1430 1733 1520 194 -76 159 C
ATOM 2101 N ASN A 274 39.064 41.790 83.394 1.00 10.07 N
ANISOU 2101 N ASN A 274 1191 1431 1202 162 -66 95 N
ATOM 2102 CA ASN A 274 39.453 43.198 83.550 1.00 9.99 C
ANISOU 2102 CA ASN A 274 1191 1428 1175 151 -75 75 C
ATOM 2103 C ASN A 274 38.651 43.801 84.702 1.00 10.44 C
ANISOU 2103 C ASN A 274 1262 1495 1209 156 -71 73 C
ATOM 2104 O ASN A 274 37.436 43.898 84.633 1.00 9.60 O
ANISOU 2104 O ASN A 274 1162 1378 1106 161 -59 74 O
ATOM 2105 CB ASN A 274 39.120 43.957 82.249 1.00 9.70 C
ANISOU 2105 CB ASN A 274 1159 1373 1152 141 -72 58 C
ATOM 2106 CG ASN A 274 40.150 43.754 81.169 1.00 10.12 C
ANISOU 2106 CG ASN A 274 1201 1421 1222 134 -78 54 C
ATOM 2107 OD1 ASN A 274 41.292 43.294 81.418 1.00 11.14 O
ANISOU 2107 OD1 ASN A 274 1320 1564 1350 134 -88 60 O
ATOM 2108 ND2 ASN A 274 39.801 44.179 79.971 1.00 10.05 N
ANISOU 2108 ND2 ASN A 274 1195 1396 1228 127 -74 43 N
ATOM 2109 N MET A 275 39.374 44.242 85.728 1.00 10.57 N
ANISOU 2109 N MET A 275 1282 1532 1203 154 -81 70 N
ATOM 2110 CA AMET A 275 38.752 44.700 86.970 0.70 11.67 C
ANISOU 2110 CA AMET A 275 1434 1683 1317 160 -78 69 C
ATOM 2111 CA BMET A 275 38.780 44.715 86.967 0.30 11.64 C
ANISOU 2111 CA BMET A 275 1430 1679 1313 160 -78 69 C
ATOM 2112 C MET A 275 37.866 45.918 86.693 1.00 11.35 C
ANISOU 2112 C MET A 275 1410 1630 1272 156 -71 50 C
ATOM 2113 O MET A 275 36.753 46.016 87.219 1.00 11.47 O
ANISOU 2113 O MET A 275 1434 1644 1279 165 -59 53 O
ATOM 2114 CB AMET A 275 39.802 45.078 88.006 0.70 12.76 C
ANISOU 2114 CB AMET A 275 1573 1845 1429 156 -93 66 C
ATOM 2115 CB BMET A 275 39.906 45.102 87.932 0.30 12.69 C
ANISOU 2115 CB BMET A 275 1564 1836 1421 155 -94 65 C
ATOM 2116 CG AMET A 275 39.176 45.556 89.301 0.70 14.20 C
ANISOU 2116 CG AMET A 275 1771 2041 1583 162 -89 64 C
ATOM 2117 CG BMET A 275 39.445 45.583 89.282 0.30 13.86 C
ANISOU 2117 CG BMET A 275 1726 2000 1540 160 -93 63 C
ATOM 2118 SD AMET A 275 40.369 46.420 90.324 0.70 15.84 S
ANISOU 2118 SD AMET A 275 1985 2274 1759 152 -108 50 S
ATOM 2119 SD BMET A 275 39.271 47.367 89.367 0.30 15.51 S
ANISOU 2119 SD BMET A 275 1957 2204 1730 148 -95 32 S
ATOM 2120 CE AMET A 275 40.509 48.006 89.475 0.70 15.94 C
ANISOU 2120 CE AMET A 275 2011 2270 1774 134 -112 18 C
ATOM 2121 CE BMET A 275 40.950 47.962 89.151 0.30 15.29 C
ANISOU 2121 CE BMET A 275 1924 2187 1698 129 -117 17 C
ATOM 2122 N LYS A 276 38.372 46.854 85.910 1.00 11.12 N
ANISOU 2122 N LYS A 276 1386 1593 1248 143 -78 31 N
ATOM 2123 CA LYS A 276 37.585 48.086 85.659 1.00 11.46 C
ANISOU 2123 CA LYS A 276 1446 1623 1287 139 -71 13 C
ATOM 2124 C LYS A 276 36.317 47.788 84.853 1.00 10.50 C
ANISOU 2124 C LYS A 276 1323 1482 1185 146 -56 19 C
ATOM 2125 O LYS A 276 35.253 48.351 85.101 1.00 10.48 O
ANISOU 2125 O LYS A 276 1331 1474 1175 153 -46 15 O
ATOM 2126 CB LYS A 276 38.408 49.134 84.988 1.00 12.52 C
ANISOU 2126 CB LYS A 276 1586 1751 1422 123 -81 -7 C
ATOM 2127 CG LYS A 276 39.595 49.574 85.819 1.00 14.95 C
ANISOU 2127 CG LYS A 276 1895 2077 1708 113 -97 -15 C
ATOM 2128 CD LYS A 276 40.331 50.711 85.119 1.00 17.66 C
ANISOU 2128 CD LYS A 276 2245 2412 2054 95 -106 -35 C
ATOM 2129 CE LYS A 276 41.595 51.102 85.886 1.00 21.65 C
ANISOU 2129 CE LYS A 276 2750 2938 2539 83 -123 -43 C
ATOM 2130 NZ LYS A 276 42.326 52.253 85.249 1.00 25.16 N
ANISOU 2130 NZ LYS A 276 3201 3374 2986 63 -132 -63 N
ATOM 2131 N ALA A 277 36.428 46.940 83.858 1.00 10.30 N
ANISOU 2131 N ALA A 277 1284 1448 1184 145 -55 28 N
ATOM 2132 CA ALA A 277 35.254 46.523 83.109 1.00 10.00 C
ANISOU 2132 CA ALA A 277 1242 1394 1164 151 -42 35 C
ATOM 2133 C ALA A 277 34.240 45.834 83.984 1.00 10.26 C
ANISOU 2133 C ALA A 277 1274 1433 1191 164 -30 51 C
ATOM 2134 O ALA A 277 33.024 46.112 83.919 1.00 10.01 O
ANISOU 2134 O ALA A 277 1248 1395 1162 170 -19 52 O
ATOM 2135 CB ALA A 277 35.689 45.563 81.999 1.00 9.81 C
ANISOU 2135 CB ALA A 277 1203 1361 1165 147 -44 43 C
ATOM 2136 N ARG A 278 34.710 44.879 84.791 1.00 10.33 N
ANISOU 2136 N ARG A 278 1275 1455 1194 170 -33 67 N
ATOM 2137 CA ARG A 278 33.822 44.150 85.686 1.00 11.21 C
ANISOU 2137 CA ARG A 278 1385 1574 1300 182 -23 85 C
ATOM 2138 C ARG A 278 33.134 45.055 86.652 1.00 11.34 C
ANISOU 2138 C ARG A 278 1417 1600 1293 188 -17 78 C
ATOM 2139 O ARG A 278 31.925 44.957 86.857 1.00 11.51 O
ANISOU 2139 O ARG A 278 1439 1618 1315 196 -3 85 O
ATOM 2140 CB ARG A 278 34.580 43.035 86.427 1.00 12.14 C
ANISOU 2140 CB ARG A 278 1494 1705 1414 187 -28 104 C
ATOM 2141 CG ARG A 278 34.756 41.867 85.536 1.00 14.42 C
ANISOU 2141 CG ARG A 278 1769 1982 1730 186 -27 116 C
ATOM 2142 CD ARG A 278 33.489 40.953 85.542 1.00 15.10 C
ANISOU 2142 CD ARG A 278 1850 2058 1828 194 -11 134 C
ATOM 2143 NE ARG A 278 33.234 40.278 86.839 1.00 17.02 N
ANISOU 2143 NE ARG A 278 2093 2317 2057 204 -6 154 N
ATOM 2144 CZ ARG A 278 33.880 39.191 87.295 1.00 19.41 C
ANISOU 2144 CZ ARG A 278 2388 2626 2363 210 -10 172 C
ATOM 2145 NH1 ARG A 278 34.832 38.576 86.578 1.00 18.01 N
ANISOU 2145 NH1 ARG A 278 2200 2440 2201 207 -17 174 N
ATOM 2146 NH2 ARG A 278 33.598 38.731 88.513 1.00 21.86 N
ANISOU 2146 NH2 ARG A 278 2698 2950 2656 220 -5 190 N
ATOM 2147 N ASN A 279 33.897 45.932 87.311 1.00 11.68 N
ANISOU 2147 N ASN A 279 1470 1654 1313 184 -27 64 N
ATOM 2148 CA ASN A 279 33.308 46.795 88.306 1.00 12.61 C
ANISOU 2148 CA ASN A 279 1604 1781 1406 190 -21 56 C
ATOM 2149 C ASN A 279 32.319 47.760 87.642 1.00 11.89 C
ANISOU 2149 C ASN A 279 1522 1673 1322 190 -11 42 C
ATOM 2150 O ASN A 279 31.284 48.138 88.250 1.00 11.88 O
ANISOU 2150 O ASN A 279 1530 1675 1309 200 2 42 O
ATOM 2151 CB ASN A 279 34.375 47.560 89.059 1.00 14.23 C
ANISOU 2151 CB ASN A 279 1819 2001 1587 183 -35 41 C
ATOM 2152 CG ASN A 279 35.059 46.706 90.121 1.00 16.60 C
ANISOU 2152 CG ASN A 279 2112 2323 1872 187 -42 57 C
ATOM 2153 OD1 ASN A 279 34.575 45.627 90.440 1.00 23.08 O
ANISOU 2153 OD1 ASN A 279 2923 3148 2698 197 -34 79 O
ATOM 2154 ND2 ASN A 279 36.253 47.133 90.566 1.00 17.09 N
ANISOU 2154 ND2 ASN A 279 2176 2399 1917 178 -58 47 N
ATOM 2155 N TYR A 280 32.643 48.221 86.430 1.00 11.52 N
ANISOU 2155 N TYR A 280 1474 1610 1292 180 -16 30 N
ATOM 2156 CA TYR A 280 31.675 49.057 85.703 1.00 11.94 C
ANISOU 2156 CA TYR A 280 1536 1647 1354 181 -6 20 C
ATOM 2157 C TYR A 280 30.374 48.288 85.437 1.00 11.93 C
ANISOU 2157 C TYR A 280 1524 1641 1368 191 8 36 C
ATOM 2158 O TYR A 280 29.273 48.774 85.787 1.00 12.03 O
ANISOU 2158 O TYR A 280 1544 1654 1374 202 21 36 O
ATOM 2159 CB TYR A 280 32.242 49.589 84.416 1.00 11.92 C
ANISOU 2159 CB TYR A 280 1532 1629 1368 169 -14 7 C
ATOM 2160 CG TYR A 280 31.215 50.432 83.683 1.00 12.53 C
ANISOU 2160 CG TYR A 280 1617 1690 1453 172 -4 -2 C
ATOM 2161 CD1 TYR A 280 30.885 51.693 84.149 1.00 12.89 C
ANISOU 2161 CD1 TYR A 280 1682 1734 1483 175 -1 -17 C
ATOM 2162 CD2 TYR A 280 30.558 49.956 82.573 1.00 12.10 C
ANISOU 2162 CD2 TYR A 280 1551 1624 1422 172 1 6 C
ATOM 2163 CE1 TYR A 280 29.944 52.462 83.506 1.00 13.17 C
ANISOU 2163 CE1 TYR A 280 1724 1754 1525 180 9 -23 C
ATOM 2164 CE2 TYR A 280 29.568 50.693 81.926 1.00 12.64 C
ANISOU 2164 CE2 TYR A 280 1626 1680 1497 177 10 1 C
ATOM 2165 CZ TYR A 280 29.277 51.950 82.408 1.00 13.02 C
ANISOU 2165 CZ TYR A 280 1691 1725 1529 181 14 -14 C
ATOM 2166 OH TYR A 280 28.265 52.693 81.787 1.00 14.39 O
ANISOU 2166 OH TYR A 280 1870 1887 1710 188 24 -18 O
ATOM 2167 N LEU A 281 30.469 47.062 84.881 1.00 11.59 N
ANISOU 2167 N LEU A 281 1464 1595 1344 189 8 52 N
ATOM 2168 CA LEU A 281 29.263 46.322 84.559 1.00 11.77 C
ANISOU 2168 CA LEU A 281 1477 1612 1382 196 21 67 C
ATOM 2169 C LEU A 281 28.444 46.045 85.811 1.00 12.57 C
ANISOU 2169 C LEU A 281 1580 1728 1468 209 32 80 C
ATOM 2170 O LEU A 281 27.211 46.138 85.793 1.00 12.99 O
ANISOU 2170 O LEU A 281 1631 1779 1524 216 46 85 O
ATOM 2171 CB LEU A 281 29.621 45.032 83.855 1.00 11.70 C
ANISOU 2171 CB LEU A 281 1452 1597 1395 191 17 81 C
ATOM 2172 CG LEU A 281 30.173 45.221 82.444 1.00 11.15 C
ANISOU 2172 CG LEU A 281 1379 1513 1345 179 9 70 C
ATOM 2173 CD1 LEU A 281 30.633 43.843 82.020 1.00 10.91 C
ANISOU 2173 CD1 LEU A 281 1335 1479 1332 176 6 84 C
ATOM 2174 CD2 LEU A 281 29.120 45.747 81.482 1.00 11.21 C
ANISOU 2174 CD2 LEU A 281 1387 1508 1365 179 17 64 C
ATOM 2175 N GLN A 282 29.127 45.704 86.896 1.00 13.06 N
ANISOU 2175 N GLN A 282 1644 1805 1512 211 27 86 N
ATOM 2176 CA GLN A 282 28.427 45.352 88.144 1.00 15.26 C
ANISOU 2176 CA GLN A 282 1924 2100 1774 223 38 100 C
ATOM 2177 C GLN A 282 27.784 46.527 88.881 1.00 15.16 C
ANISOU 2177 C GLN A 282 1928 2094 1738 232 47 88 C
ATOM 2178 O GLN A 282 26.973 46.329 89.757 1.00 17.45 O
ANISOU 2178 O GLN A 282 2219 2396 2016 243 59 99 O
ATOM 2179 CB GLN A 282 29.387 44.519 89.016 1.00 17.17 C
ANISOU 2179 CB GLN A 282 2163 2357 2005 224 30 113 C
ATOM 2180 CG GLN A 282 29.633 43.159 88.335 1.00 19.83 C
ANISOU 2180 CG GLN A 282 2483 2685 2367 220 28 131 C
ATOM 2181 CD GLN A 282 30.715 42.253 88.914 1.00 22.94 C
ANISOU 2181 CD GLN A 282 2871 3090 2756 220 18 144 C
ATOM 2182 OE1 GLN A 282 31.007 41.172 88.315 1.00 26.08 O
ANISOU 2182 OE1 GLN A 282 3256 3478 3175 217 17 157 O
ATOM 2183 NE2 GLN A 282 31.364 42.672 90.006 1.00 24.60 N
ANISOU 2183 NE2 GLN A 282 3088 3319 2939 223 11 141 N
ATOM 2184 N SER A 283 28.049 47.727 88.436 1.00 14.87 N
ANISOU 2184 N SER A 283 1903 2048 1697 227 42 65 N
ATOM 2185 CA SER A 283 27.499 48.934 89.096 1.00 15.37 C
ANISOU 2185 CA SER A 283 1984 2115 1739 236 49 51 C
ATOM 2186 C SER A 283 26.169 49.307 88.472 1.00 15.99 C
ANISOU 2186 C SER A 283 2061 2183 1831 244 64 51 C
ATOM 2187 O SER A 283 25.465 50.185 88.936 1.00 18.15 O
ANISOU 2187 O SER A 283 2347 2458 2091 254 75 42 O
ATOM 2188 CB SER A 283 28.477 50.092 88.916 1.00 14.85 C
ANISOU 2188 CB SER A 283 1935 2044 1664 226 36 26 C
ATOM 2189 OG SER A 283 28.527 50.659 87.618 1.00 14.09 O
ANISOU 2189 OG SER A 283 1838 1927 1588 217 33 14 O
ATOM 2190 N LEU A 284 25.865 48.711 87.324 1.00 15.03 N
ANISOU 2190 N LEU A 284 1925 2049 1737 238 64 60 N
ATOM 2191 CA LEU A 284 24.714 49.192 86.518 1.00 15.68 C
ANISOU 2191 CA LEU A 284 2005 2120 1834 243 75 58 C
ATOM 2192 C LEU A 284 23.412 48.564 87.048 1.00 14.87 C
ANISOU 2192 C LEU A 284 1892 2028 1732 256 92 77 C
ATOM 2193 O LEU A 284 23.441 47.491 87.669 1.00 16.35 O
ANISOU 2193 O LEU A 284 2070 2226 1917 257 94 95 O
ATOM 2194 CB LEU A 284 24.913 48.798 85.048 1.00 15.05 C
ANISOU 2194 CB LEU A 284 1912 2024 1781 232 68 59 C
ATOM 2195 CG LEU A 284 26.168 49.387 84.371 1.00 15.36 C
ANISOU 2195 CG LEU A 284 1960 2054 1823 218 52 41 C
ATOM 2196 CD1 LEU A 284 26.234 48.898 82.956 1.00 15.55 C
ANISOU 2196 CD1 LEU A 284 1971 2064 1873 209 47 44 C
ATOM 2197 CD2 LEU A 284 26.149 50.921 84.455 1.00 15.95 C
ANISOU 2197 CD2 LEU A 284 2054 2122 1884 221 53 21 C
ATOM 2198 N PRO A 285 22.276 49.178 86.695 1.00 16.27 N
ANISOU 2198 N PRO A 285 2068 2200 1913 265 104 76 N
ATOM 2199 CA PRO A 285 21.021 48.608 87.209 1.00 16.67 C
ANISOU 2199 CA PRO A 285 2108 2262 1965 276 121 95 C
ATOM 2200 C PRO A 285 20.704 47.282 86.587 1.00 15.50 C
ANISOU 2200 C PRO A 285 1938 2112 1840 268 121 115 C
ATOM 2201 O PRO A 285 21.027 47.051 85.414 1.00 16.17 O
ANISOU 2201 O PRO A 285 2016 2183 1946 256 111 111 O
ATOM 2202 CB PRO A 285 19.953 49.651 86.806 1.00 17.17 C
ANISOU 2202 CB PRO A 285 2174 2320 2029 288 132 87 C
ATOM 2203 CG PRO A 285 20.687 50.938 86.590 1.00 18.18 C
ANISOU 2203 CG PRO A 285 2323 2436 2148 286 124 62 C
ATOM 2204 CD PRO A 285 22.121 50.575 86.208 1.00 16.60 C
ANISOU 2204 CD PRO A 285 2125 2230 1953 269 105 56 C
ATOM 2205 N SER A 286 20.157 46.374 87.363 1.00 15.98 N
ANISOU 2205 N SER A 286 1989 2186 1898 273 131 135 N
ATOM 2206 CA ASER A 286 19.763 45.068 86.866 0.50 16.54 C
ANISOU 2206 CA ASER A 286 2040 2254 1991 264 132 155 C
ATOM 2207 CA BSER A 286 19.763 45.071 86.852 0.50 16.96 C
ANISOU 2207 CA BSER A 286 2093 2307 2045 264 132 155 C
ATOM 2208 C SER A 286 18.649 45.236 85.818 1.00 16.21 C
ANISOU 2208 C SER A 286 1986 2205 1970 264 138 156 C
ATOM 2209 O SER A 286 17.678 45.947 86.038 1.00 18.48 O
ANISOU 2209 O SER A 286 2274 2499 2250 276 151 156 O
ATOM 2210 CB ASER A 286 19.299 44.180 88.045 0.50 17.71 C
ANISOU 2210 CB ASER A 286 2181 2418 2129 271 144 177 C
ATOM 2211 CB BSER A 286 19.307 44.166 88.007 0.50 18.68 C
ANISOU 2211 CB BSER A 286 2304 2541 2253 271 144 177 C
ATOM 2212 OG ASER A 286 18.737 42.968 87.582 0.50 19.38 O
ANISOU 2212 OG ASER A 286 2374 2626 2364 263 148 197 O
ATOM 2213 OG BSER A 286 20.362 43.969 88.916 0.50 22.07 O
ANISOU 2213 OG BSER A 286 2744 2978 2664 271 136 176 O
ATOM 2214 N LYS A 287 18.785 44.569 84.663 1.00 14.11 N
ANISOU 2214 N LYS A 287 1708 1925 1727 250 130 159 N
ATOM 2215 CA LYS A 287 17.784 44.704 83.583 1.00 13.98 C
ANISOU 2215 CA LYS A 287 1679 1902 1729 247 133 160 C
ATOM 2216 C LYS A 287 17.738 43.437 82.798 1.00 13.01 C
ANISOU 2216 C LYS A 287 1541 1772 1631 232 129 172 C
ATOM 2217 O LYS A 287 18.759 42.899 82.471 1.00 13.04 O
ANISOU 2217 O LYS A 287 1547 1767 1641 222 117 169 O
ATOM 2218 CB LYS A 287 18.121 45.861 82.623 1.00 14.27 C
ANISOU 2218 CB LYS A 287 1725 1927 1768 246 125 139 C
ATOM 2219 CG LYS A 287 17.002 46.109 81.611 1.00 15.30 C
ANISOU 2219 CG LYS A 287 1843 2055 1915 247 129 142 C
ATOM 2220 CD LYS A 287 17.206 47.382 80.798 1.00 16.46 C
ANISOU 2220 CD LYS A 287 2001 2192 2061 249 123 123 C
ATOM 2221 CE LYS A 287 15.996 47.627 79.907 1.00 17.22 C
ANISOU 2221 CE LYS A 287 2083 2288 2171 252 129 128 C
ATOM 2222 NZ LYS A 287 16.188 48.838 79.053 1.00 17.60 N
ANISOU 2222 NZ LYS A 287 2143 2326 2219 255 123 112 N
ATOM 2223 N THR A 288 16.516 42.986 82.490 1.00 12.28 N
ANISOU 2223 N THR A 288 1432 1684 1552 231 138 186 N
ATOM 2224 CA THR A 288 16.290 41.847 81.658 1.00 13.06 C
ANISOU 2224 CA THR A 288 1515 1773 1674 215 134 196 C
ATOM 2225 C THR A 288 16.313 42.245 80.168 1.00 12.26 C
ANISOU 2225 C THR A 288 1411 1660 1588 206 124 182 C
ATOM 2226 O THR A 288 15.873 43.320 79.780 1.00 12.47 O
ANISOU 2226 O THR A 288 1440 1688 1610 214 125 173 O
ATOM 2227 CB THR A 288 14.925 41.226 81.986 1.00 13.23 C
ANISOU 2227 CB THR A 288 1518 1806 1703 216 148 217 C
ATOM 2228 OG1 THR A 288 14.945 40.848 83.368 1.00 14.87 O
ANISOU 2228 OG1 THR A 288 1729 2026 1895 224 158 230 O
ATOM 2229 CG2 THR A 288 14.663 39.991 81.181 1.00 13.64 C
ANISOU 2229 CG2 THR A 288 1556 1849 1779 198 144 227 C
ATOM 2230 N LYS A 289 16.870 41.347 79.390 1.00 12.87 N
ANISOU 2230 N LYS A 289 1484 1724 1681 191 114 182 N
ATOM 2231 CA ALYS A 289 16.897 41.457 77.925 0.70 13.82 C
ANISOU 2231 CA ALYS A 289 1600 1834 1818 180 104 171 C
ATOM 2232 CA BLYS A 289 16.905 41.453 77.930 0.30 13.67 C
ANISOU 2232 CA BLYS A 289 1581 1815 1799 180 104 171 C
ATOM 2233 C LYS A 289 15.559 41.912 77.384 1.00 13.79 C
ANISOU 2233 C LYS A 289 1583 1836 1819 182 110 175 C
ATOM 2234 O LYS A 289 14.486 41.378 77.765 1.00 14.70 O
ANISOU 2234 O LYS A 289 1684 1961 1939 183 120 191 O
ATOM 2235 CB ALYS A 289 17.231 40.089 77.343 0.70 15.26 C
ANISOU 2235 CB ALYS A 289 1776 2005 2019 164 98 177 C
ATOM 2236 CB BLYS A 289 17.272 40.082 77.354 0.30 14.43 C
ANISOU 2236 CB BLYS A 289 1671 1899 1914 164 98 177 C
ATOM 2237 CG ALYS A 289 17.050 39.959 75.836 0.70 16.03 C
ANISOU 2237 CG ALYS A 289 1866 2092 2134 150 90 169 C
ATOM 2238 CG BLYS A 289 17.129 39.912 75.847 0.30 14.92 C
ANISOU 2238 CG BLYS A 289 1726 1950 1993 150 89 168 C
ATOM 2239 CD ALYS A 289 17.329 38.521 75.383 0.70 16.07 C
ANISOU 2239 CD ALYS A 289 1864 2084 2156 134 86 175 C
ATOM 2240 CD BLYS A 289 17.237 38.431 75.496 0.30 15.19 C
ANISOU 2240 CD BLYS A 289 1752 1973 2045 135 87 177 C
ATOM 2241 CE ALYS A 289 17.813 38.410 73.920 0.70 16.92 C
ANISOU 2241 CE ALYS A 289 1974 2179 2277 122 74 160 C
ATOM 2242 CE BLYS A 289 17.201 38.143 73.998 0.30 15.56 C
ANISOU 2242 CE BLYS A 289 1794 2009 2108 120 78 167 C
ATOM 2243 NZ ALYS A 289 18.914 39.366 73.610 0.70 16.15 N
ANISOU 2243 NZ ALYS A 289 1890 2078 2169 127 65 143 N
ATOM 2244 NZ BLYS A 289 17.608 36.739 73.711 0.30 15.88 N
ANISOU 2244 NZ BLYS A 289 1833 2036 2165 106 75 172 N
ATOM 2245 N VAL A 290 15.580 42.897 76.492 1.00 14.23 N
ANISOU 2245 N VAL A 290 1644 1889 1875 184 104 161 N
ATOM 2246 CA VAL A 290 14.342 43.383 75.839 1.00 14.96 C
ANISOU 2246 CA VAL A 290 1724 1988 1974 187 108 164 C
ATOM 2247 C VAL A 290 14.028 42.429 74.702 1.00 14.76 C
ANISOU 2247 C VAL A 290 1683 1956 1968 169 100 167 C
ATOM 2248 O VAL A 290 14.896 42.130 73.864 1.00 14.51 O
ANISOU 2248 O VAL A 290 1658 1912 1945 157 89 157 O
ATOM 2249 CB VAL A 290 14.516 44.814 75.304 1.00 15.69 C
ANISOU 2249 CB VAL A 290 1827 2078 2058 197 104 148 C
ATOM 2250 CG1 VAL A 290 13.276 45.304 74.557 1.00 16.14 C
ANISOU 2250 CG1 VAL A 290 1869 2141 2121 201 107 153 C
ATOM 2251 CG2 VAL A 290 14.793 45.791 76.426 1.00 16.84 C
ANISOU 2251 CG2 VAL A 290 1988 2227 2182 215 111 143 C
ATOM 2252 N ALA A 291 12.770 41.950 74.639 1.00 15.24 N
ANISOU 2252 N ALA A 291 1724 2027 2038 165 107 182 N
ATOM 2253 CA ALA A 291 12.401 40.937 73.661 1.00 15.68 C
ANISOU 2253 CA ALA A 291 1766 2078 2113 145 101 186 C
ATOM 2254 C ALA A 291 12.498 41.547 72.261 1.00 14.50 C
ANISOU 2254 C ALA A 291 1617 1923 1968 140 89 172 C
ATOM 2255 O ALA A 291 11.948 42.605 71.999 1.00 15.13 O
ANISOU 2255 O ALA A 291 1696 2012 2043 152 91 169 O
ATOM 2256 CB ALA A 291 10.990 40.457 73.902 1.00 16.70 C
ANISOU 2256 CB ALA A 291 1873 2221 2249 143 110 204 C
ATOM 2257 N TRP A 292 13.117 40.838 71.341 1.00 15.57 N
ANISOU 2257 N TRP A 292 1755 2047 2116 124 78 164 N
ATOM 2258 CA TRP A 292 13.255 41.375 69.967 1.00 14.40 C
ANISOU 2258 CA TRP A 292 1608 1894 1971 118 67 151 C
ATOM 2259 C TRP A 292 11.900 41.615 69.336 1.00 15.02 C
ANISOU 2259 C TRP A 292 1668 1986 2055 116 67 158 C
ATOM 2260 O TRP A 292 11.754 42.608 68.650 1.00 12.94 O
ANISOU 2260 O TRP A 292 1406 1726 1786 123 63 151 O
ATOM 2261 CB TRP A 292 14.007 40.404 69.096 1.00 14.75 C
ANISOU 2261 CB TRP A 292 1655 1924 2027 99 56 143 C
ATOM 2262 CG TRP A 292 15.395 40.173 69.571 1.00 14.40 C
ANISOU 2262 CG TRP A 292 1627 1867 1978 101 55 135 C
ATOM 2263 CD1 TRP A 292 15.952 38.986 70.005 1.00 15.29 C
ANISOU 2263 CD1 TRP A 292 1742 1970 2098 93 56 140 C
ATOM 2264 CD2 TRP A 292 16.446 41.120 69.553 1.00 14.61 C
ANISOU 2264 CD2 TRP A 292 1670 1889 1993 110 50 122 C
ATOM 2265 NE1 TRP A 292 17.253 39.195 70.364 1.00 14.78 N
ANISOU 2265 NE1 TRP A 292 1692 1897 2025 99 53 131 N
ATOM 2266 CE2 TRP A 292 17.589 40.489 70.073 1.00 13.87 C
ANISOU 2266 CE2 TRP A 292 1586 1786 1899 108 49 120 C
ATOM 2267 CE3 TRP A 292 16.505 42.468 69.215 1.00 13.58 C
ANISOU 2267 CE3 TRP A 292 1547 1762 1852 120 48 113 C
ATOM 2268 CZ2 TRP A 292 18.800 41.148 70.203 1.00 13.39 C
ANISOU 2268 CZ2 TRP A 292 1540 1719 1827 114 45 108 C
ATOM 2269 CZ3 TRP A 292 17.710 43.135 69.373 1.00 14.67 C
ANISOU 2269 CZ3 TRP A 292 1701 1892 1979 126 44 101 C
ATOM 2270 CH2 TRP A 292 18.818 42.490 69.850 1.00 13.99 C
ANISOU 2270 CH2 TRP A 292 1623 1799 1893 122 42 99 C
ATOM 2271 N ALA A 293 10.945 40.724 69.549 1.00 15.80 N
ANISOU 2271 N ALA A 293 1748 2092 2163 107 72 173 N
ATOM 2272 CA ALA A 293 9.600 40.960 69.054 1.00 17.31 C
ANISOU 2272 CA ALA A 293 1919 2300 2359 106 73 181 C
ATOM 2273 C ALA A 293 8.942 42.238 69.564 1.00 17.57 C
ANISOU 2273 C ALA A 293 1949 2347 2379 130 82 187 C
ATOM 2274 O ALA A 293 8.041 42.749 68.907 1.00 17.66 O
ANISOU 2274 O ALA A 293 1948 2371 2393 133 80 190 O
ATOM 2275 CB ALA A 293 8.693 39.765 69.329 1.00 18.51 C
ANISOU 2275 CB ALA A 293 2052 2458 2524 92 78 197 C
ATOM 2276 N LYS A 294 9.309 42.732 70.742 1.00 18.47 N
ANISOU 2276 N LYS A 294 2076 2461 2481 147 93 188 N
ATOM 2277 CA LYS A 294 8.781 44.003 71.230 1.00 19.20 C
ANISOU 2277 CA LYS A 294 2170 2565 2561 171 102 190 C
ATOM 2278 C LYS A 294 9.445 45.223 70.583 1.00 18.28 C
ANISOU 2278 C LYS A 294 2071 2440 2436 180 95 174 C
ATOM 2279 O LYS A 294 8.796 46.211 70.295 1.00 19.42 O
ANISOU 2279 O LYS A 294 2211 2591 2576 194 97 175 O
ATOM 2280 CB LYS A 294 8.885 44.074 72.746 1.00 23.04 C
ANISOU 2280 CB LYS A 294 2664 3055 3035 185 116 196 C
ATOM 2281 CG LYS A 294 8.070 42.973 73.430 1.00 29.13 C
ANISOU 2281 CG LYS A 294 3418 3838 3814 177 125 215 C
ATOM 2282 CD LYS A 294 7.548 43.407 74.795 1.00 34.64 C
ANISOU 2282 CD LYS A 294 4115 4549 4499 197 143 226 C
ATOM 2283 CE LYS A 294 7.442 42.211 75.732 1.00 40.70 C
ANISOU 2283 CE LYS A 294 4875 5319 5269 189 151 241 C
ATOM 2284 NZ LYS A 294 6.430 41.217 75.273 1.00 41.33 N
ANISOU 2284 NZ LYS A 294 4929 5407 5366 171 151 256 N
ATOM 2285 N LEU A 295 10.718 45.089 70.230 1.00 16.43 N
ANISOU 2285 N LEU A 295 1854 2189 2201 171 85 160 N
ATOM 2286 CA LEU A 295 11.436 46.120 69.535 1.00 16.94 C
ANISOU 2286 CA LEU A 295 1934 2244 2260 176 77 145 C
ATOM 2287 C LEU A 295 11.082 46.185 68.054 1.00 15.42 C
ANISOU 2287 C LEU A 295 1731 2052 2075 166 66 142 C
ATOM 2288 O LEU A 295 11.115 47.274 67.436 1.00 16.01 O
ANISOU 2288 O LEU A 295 1813 2126 2145 176 63 136 O
ATOM 2289 CB LEU A 295 12.916 45.862 69.708 1.00 18.41 C
ANISOU 2289 CB LEU A 295 2139 2414 2442 169 71 132 C
ATOM 2290 CG LEU A 295 13.321 46.113 71.136 1.00 21.94 C
ANISOU 2290 CG LEU A 295 2599 2862 2877 182 81 133 C
ATOM 2291 CD1 LEU A 295 14.735 45.597 71.331 1.00 22.78 C
ANISOU 2291 CD1 LEU A 295 2718 2955 2981 173 74 123 C
ATOM 2292 CD2 LEU A 295 13.197 47.590 71.461 1.00 22.77 C
ANISOU 2292 CD2 LEU A 295 2716 2968 2968 202 86 128 C
ATOM 2293 N PHE A 296 10.711 45.027 67.503 1.00 15.42 N
ANISOU 2293 N PHE A 296 1716 2055 2088 147 60 148 N
ATOM 2294 CA PHE A 296 10.500 44.877 66.058 1.00 14.93 C
ANISOU 2294 CA PHE A 296 1645 1993 2034 134 48 143 C
ATOM 2295 C PHE A 296 9.183 44.143 65.840 1.00 15.09 C
ANISOU 2295 C PHE A 296 1639 2029 2064 124 49 157 C
ATOM 2296 O PHE A 296 9.158 43.026 65.348 1.00 14.69 O
ANISOU 2296 O PHE A 296 1581 1976 2025 103 42 157 O
ATOM 2297 CB PHE A 296 11.675 44.092 65.407 1.00 14.56 C
ANISOU 2297 CB PHE A 296 1610 1931 1993 115 37 130 C
ATOM 2298 CG PHE A 296 13.006 44.770 65.504 1.00 14.48 C
ANISOU 2298 CG PHE A 296 1622 1907 1973 122 35 116 C
ATOM 2299 CD1 PHE A 296 13.423 45.709 64.557 1.00 14.99 C
ANISOU 2299 CD1 PHE A 296 1696 1968 2033 125 28 106 C
ATOM 2300 CD2 PHE A 296 13.886 44.429 66.501 1.00 15.23 C
ANISOU 2300 CD2 PHE A 296 1729 1993 2065 124 40 114 C
ATOM 2301 CE1 PHE A 296 14.662 46.305 64.635 1.00 14.68 C
ANISOU 2301 CE1 PHE A 296 1677 1916 1986 129 26 94 C
ATOM 2302 CE2 PHE A 296 15.127 45.053 66.605 1.00 14.91 C
ANISOU 2302 CE2 PHE A 296 1708 1941 2015 129 37 101 C
ATOM 2303 CZ PHE A 296 15.504 45.999 65.695 1.00 14.17 C
ANISOU 2303 CZ PHE A 296 1623 1844 1918 131 30 92 C
ATOM 2304 N PRO A 297 8.078 44.781 66.197 1.00 15.73 N
ANISOU 2304 N PRO A 297 1707 2127 2142 139 57 170 N
ATOM 2305 CA PRO A 297 6.816 44.066 66.259 1.00 17.45 C
ANISOU 2305 CA PRO A 297 1900 2362 2370 131 60 185 C
ATOM 2306 C PRO A 297 6.242 43.694 64.909 1.00 18.02 C
ANISOU 2306 C PRO A 297 1955 2441 2451 114 47 185 C
ATOM 2307 O PRO A 297 5.325 42.853 64.824 1.00 19.48 O
ANISOU 2307 O PRO A 297 2119 2638 2646 100 47 196 O
ATOM 2308 CB PRO A 297 5.908 45.048 67.014 1.00 16.97 C
ANISOU 2308 CB PRO A 297 1831 2317 2301 156 74 197 C
ATOM 2309 CG PRO A 297 6.451 46.397 66.687 1.00 16.78 C
ANISOU 2309 CG PRO A 297 1824 2285 2265 174 72 187 C
ATOM 2310 CD PRO A 297 7.945 46.176 66.661 1.00 16.29 C
ANISOU 2310 CD PRO A 297 1787 2201 2201 165 65 170 C
ATOM 2311 N LYS A 298 6.762 44.253 63.836 1.00 17.82 N
ANISOU 2311 N LYS A 298 1939 2409 2421 113 36 173 N
ATOM 2312 CA LYS A 298 6.224 43.878 62.515 1.00 19.89 C
ANISOU 2312 CA LYS A 298 2187 2681 2691 95 22 173 C
ATOM 2313 C LYS A 298 7.196 43.045 61.676 1.00 18.74 C
ANISOU 2313 C LYS A 298 2052 2519 2550 73 10 157 C
ATOM 2314 O LYS A 298 6.986 42.865 60.486 1.00 19.86 O
ANISOU 2314 O LYS A 298 2187 2666 2694 59 -2 152 O
ATOM 2315 CB LYS A 298 5.780 45.122 61.728 1.00 22.52 C
ANISOU 2315 CB LYS A 298 2516 3025 3016 110 18 174 C
ATOM 2316 CG LYS A 298 4.876 46.090 62.512 1.00 25.14 C
ANISOU 2316 CG LYS A 298 2839 3372 3343 136 30 189 C
ATOM 2317 CD LYS A 298 5.197 47.538 62.175 1.00 29.21 C
ANISOU 2317 CD LYS A 298 3368 3882 3847 158 30 184 C
ATOM 2318 CE LYS A 298 6.637 47.964 62.507 1.00 31.88 C
ANISOU 2318 CE LYS A 298 3738 4197 4178 163 32 168 C
ATOM 2319 NZ LYS A 298 6.901 48.624 63.836 1.00 30.64 N
ANISOU 2319 NZ LYS A 298 3595 4034 4013 184 47 169 N
ATOM 2320 N SER A 299 8.267 42.562 62.280 1.00 16.49 N
ANISOU 2320 N SER A 299 1785 2216 2265 70 14 149 N
ATOM 2321 CA SER A 299 9.309 41.839 61.543 1.00 14.66 C
ANISOU 2321 CA SER A 299 1567 1967 2037 52 4 133 C
ATOM 2322 C SER A 299 9.083 40.338 61.588 1.00 14.48 C
ANISOU 2322 C SER A 299 1535 1940 2028 30 3 135 C
ATOM 2323 O SER A 299 8.535 39.810 62.552 1.00 14.01 O
ANISOU 2323 O SER A 299 1466 1884 1974 30 12 148 O
ATOM 2324 CB SER A 299 10.660 42.182 62.165 1.00 14.23 C
ANISOU 2324 CB SER A 299 1535 1895 1975 63 9 124 C
ATOM 2325 OG SER A 299 10.918 43.573 62.029 1.00 13.80 O
ANISOU 2325 OG SER A 299 1492 1843 1910 81 9 120 O
ATOM 2326 N ASP A 300 9.611 39.630 60.599 1.00 14.86 N
ANISOU 2326 N ASP A 300 1588 1977 2080 11 -7 122 N
ATOM 2327 CA ASP A 300 9.482 38.213 60.504 1.00 16.10 C
ANISOU 2327 CA ASP A 300 1740 2127 2251 -11 -9 122 C
ATOM 2328 C ASP A 300 10.166 37.507 61.680 1.00 15.62 C
ANISOU 2328 C ASP A 300 1689 2049 2194 -9 1 125 C
ATOM 2329 O ASP A 300 11.295 37.867 62.045 1.00 13.70 O
ANISOU 2329 O ASP A 300 1465 1795 1945 3 4 117 O
ATOM 2330 CB ASP A 300 10.078 37.746 59.179 1.00 19.65 C
ANISOU 2330 CB ASP A 300 2198 2567 2702 -29 -22 104 C
ATOM 2331 CG ASP A 300 9.973 36.260 58.995 1.00 23.67 C
ANISOU 2331 CG ASP A 300 2703 3064 3225 -53 -24 101 C
ATOM 2332 OD1 ASP A 300 8.929 35.794 58.492 1.00 23.20 O
ANISOU 2332 OD1 ASP A 300 2627 3017 3172 -69 -30 105 O
ATOM 2333 OD2 ASP A 300 10.904 35.542 59.396 1.00 24.22 O
ANISOU 2333 OD2 ASP A 300 2788 3115 3300 -55 -20 95 O
ATOM 2334 N SER A 301 9.503 36.548 62.297 1.00 15.25 N
ANISOU 2334 N SER A 301 1632 2004 2159 -20 7 137 N
ATOM 2335 CA SER A 301 10.051 35.795 63.443 1.00 15.53 C
ANISOU 2335 CA SER A 301 1676 2026 2200 -18 17 143 C
ATOM 2336 C SER A 301 11.389 35.121 63.167 1.00 14.27 C
ANISOU 2336 C SER A 301 1536 1843 2043 -24 14 128 C
ATOM 2337 O SER A 301 12.214 35.056 64.053 1.00 14.68 O
ANISOU 2337 O SER A 301 1600 1885 2093 -13 20 130 O
ATOM 2338 CB SER A 301 9.042 34.748 63.968 1.00 17.49 C
ANISOU 2338 CB SER A 301 1907 2277 2460 -33 23 158 C
ATOM 2339 OG SER A 301 8.827 33.775 62.972 1.00 21.14 O
ANISOU 2339 OG SER A 301 2365 2732 2934 -58 14 150 O
ATOM 2340 N LYS A 302 11.562 34.589 61.959 1.00 13.77 N
ANISOU 2340 N LYS A 302 1474 1771 1985 -42 3 115 N
ATOM 2341 CA LYS A 302 12.842 33.985 61.603 1.00 13.81 C
ANISOU 2341 CA LYS A 302 1498 1755 1994 -46 0 100 C
ATOM 2342 C LYS A 302 13.960 35.002 61.488 1.00 12.94 C
ANISOU 2342 C LYS A 302 1403 1643 1870 -29 -1 90 C
ATOM 2343 O LYS A 302 15.081 34.745 61.949 1.00 12.08 O
ANISOU 2343 O LYS A 302 1308 1519 1761 -22 2 85 O
ATOM 2344 CB LYS A 302 12.763 33.142 60.328 1.00 14.92 C
ANISOU 2344 CB LYS A 302 1638 1887 2143 -69 -10 87 C
ATOM 2345 CG LYS A 302 11.810 31.939 60.467 1.00 16.86 C
ANISOU 2345 CG LYS A 302 1872 2130 2404 -90 -8 95 C
ATOM 2346 CD LYS A 302 11.727 31.197 59.165 1.00 18.51 C
ANISOU 2346 CD LYS A 302 2082 2331 2619 -113 -19 80 C
ATOM 2347 CE LYS A 302 10.892 31.939 58.171 1.00 20.67 C
ANISOU 2347 CE LYS A 302 2342 2626 2885 -118 -29 76 C
ATOM 2348 NZ LYS A 302 10.088 30.902 57.469 1.00 23.50 N
ANISOU 2348 NZ LYS A 302 2691 2984 3255 -146 -36 73 N
ATOM 2349 N ALA A 303 13.661 36.177 60.950 1.00 12.32 N
ANISOU 2349 N ALA A 303 1321 1579 1781 -21 -6 87 N
ATOM 2350 CA ALA A 303 14.665 37.264 60.931 1.00 11.78 C
ANISOU 2350 CA ALA A 303 1267 1509 1700 -4 -7 79 C
ATOM 2351 C ALA A 303 15.079 37.591 62.361 1.00 11.23 C
ANISOU 2351 C ALA A 303 1203 1438 1625 13 3 88 C
ATOM 2352 O ALA A 303 16.229 37.844 62.622 1.00 10.71 O
ANISOU 2352 O ALA A 303 1152 1363 1554 21 4 81 O
ATOM 2353 CB ALA A 303 14.122 38.473 60.244 1.00 11.36 C
ANISOU 2353 CB ALA A 303 1208 1471 1636 3 -12 78 C
ATOM 2354 N LEU A 304 14.129 37.662 63.291 1.00 11.23 N
ANISOU 2354 N LEU A 304 1192 1448 1626 19 11 103 N
ATOM 2355 CA LEU A 304 14.456 38.016 64.675 1.00 10.98 C
ANISOU 2355 CA LEU A 304 1167 1417 1587 36 21 112 C
ATOM 2356 C LEU A 304 15.227 36.967 65.399 1.00 11.12 C
ANISOU 2356 C LEU A 304 1192 1421 1611 32 26 114 C
ATOM 2357 O LEU A 304 16.070 37.285 66.222 1.00 11.20 O
ANISOU 2357 O LEU A 304 1214 1428 1614 45 30 114 O
ATOM 2358 CB LEU A 304 13.178 38.357 65.412 1.00 11.24 C
ANISOU 2358 CB LEU A 304 1186 1468 1619 43 29 128 C
ATOM 2359 CG LEU A 304 12.459 39.606 64.884 1.00 11.73 C
ANISOU 2359 CG LEU A 304 1240 1544 1672 53 27 128 C
ATOM 2360 CD1 LEU A 304 11.268 39.976 65.770 1.00 12.75 C
ANISOU 2360 CD1 LEU A 304 1355 1690 1798 64 37 145 C
ATOM 2361 CD2 LEU A 304 13.342 40.821 64.692 1.00 11.91 C
ANISOU 2361 CD2 LEU A 304 1279 1563 1682 67 24 116 C
ATOM 2362 N ASP A 305 14.990 35.702 65.045 1.00 10.83 N
ANISOU 2362 N ASP A 305 1150 1375 1589 15 24 115 N
ATOM 2363 CA ASP A 305 15.748 34.615 65.616 1.00 11.44 C
ANISOU 2363 CA ASP A 305 1236 1436 1674 11 28 118 C
ATOM 2364 C ASP A 305 17.191 34.740 65.176 1.00 11.24 C
ANISOU 2364 C ASP A 305 1227 1399 1645 15 23 102 C
ATOM 2365 O ASP A 305 18.092 34.582 65.992 1.00 11.72 O
ANISOU 2365 O ASP A 305 1297 1453 1703 25 27 105 O
ATOM 2366 CB ASP A 305 15.179 33.245 65.279 1.00 12.50 C
ANISOU 2366 CB ASP A 305 1363 1561 1825 -9 28 122 C
ATOM 2367 CG ASP A 305 15.962 32.154 65.959 1.00 14.31 C
ANISOU 2367 CG ASP A 305 1601 1772 2062 -10 34 126 C
ATOM 2368 OD1 ASP A 305 15.793 31.994 67.215 1.00 17.69 O
ANISOU 2368 OD1 ASP A 305 2028 2203 2489 -1 43 143 O
ATOM 2369 OD2 ASP A 305 16.862 31.549 65.332 1.00 14.65 O
ANISOU 2369 OD2 ASP A 305 1656 1799 2112 -16 29 114 O
ATOM 2370 N LEU A 306 17.409 35.027 63.890 1.00 10.59 N
ANISOU 2370 N LEU A 306 1147 1315 1562 8 14 87 N
ATOM 2371 CA LEU A 306 18.755 35.150 63.392 1.00 10.38 C
ANISOU 2371 CA LEU A 306 1133 1277 1531 11 9 73 C
ATOM 2372 C LEU A 306 19.413 36.403 64.006 1.00 9.53 C
ANISOU 2372 C LEU A 306 1033 1178 1408 29 11 72 C
ATOM 2373 O LEU A 306 20.572 36.373 64.417 1.00 9.02 O
ANISOU 2373 O LEU A 306 980 1107 1342 36 11 69 O
ATOM 2374 CB LEU A 306 18.773 35.173 61.855 1.00 10.46 C
ANISOU 2374 CB LEU A 306 1144 1286 1543 -1 0 58 C
ATOM 2375 CG LEU A 306 20.139 35.271 61.193 1.00 10.88 C
ANISOU 2375 CG LEU A 306 1210 1330 1593 1 -4 42 C
ATOM 2376 CD1 LEU A 306 21.081 34.273 61.726 1.00 10.89 C
ANISOU 2376 CD1 LEU A 306 1220 1316 1603 2 0 43 C
ATOM 2377 CD2 LEU A 306 19.969 35.115 59.694 1.00 11.11 C
ANISOU 2377 CD2 LEU A 306 1239 1358 1624 -13 -12 29 C
ATOM 2378 N LEU A 307 18.682 37.509 64.108 1.00 9.80 N
ANISOU 2378 N LEU A 307 1063 1227 1434 37 11 76 N
ATOM 2379 CA LEU A 307 19.158 38.726 64.752 1.00 9.85 C
ANISOU 2379 CA LEU A 307 1078 1239 1426 53 13 75 C
ATOM 2380 C LEU A 307 19.642 38.395 66.161 1.00 11.03 C
ANISOU 2380 C LEU A 307 1232 1387 1573 62 20 84 C
ATOM 2381 O LEU A 307 20.740 38.858 66.570 1.00 10.68 O
ANISOU 2381 O LEU A 307 1198 1339 1519 71 19 78 O
ATOM 2382 CB LEU A 307 18.058 39.795 64.826 1.00 10.21 C
ANISOU 2382 CB LEU A 307 1115 1299 1463 61 15 81 C
ATOM 2383 CG LEU A 307 18.446 41.094 65.484 1.00 10.38 C
ANISOU 2383 CG LEU A 307 1147 1326 1471 78 18 80 C
ATOM 2384 CD1 LEU A 307 19.506 41.801 64.639 1.00 10.56 C
ANISOU 2384 CD1 LEU A 307 1182 1343 1489 78 10 65 C
ATOM 2385 CD2 LEU A 307 17.221 41.967 65.603 1.00 11.48 C
ANISOU 2385 CD2 LEU A 307 1278 1479 1605 87 22 87 C
ATOM 2386 N ASP A 308 18.821 37.619 66.905 1.00 10.93 N
ANISOU 2386 N ASP A 308 1210 1375 1566 60 27 99 N
ATOM 2387 CA ASP A 308 19.160 37.230 68.275 1.00 11.69 C
ANISOU 2387 CA ASP A 308 1310 1472 1660 69 35 110 C
ATOM 2388 C ASP A 308 20.514 36.506 68.385 1.00 11.53 C
ANISOU 2388 C ASP A 308 1299 1438 1643 68 32 105 C
ATOM 2389 O ASP A 308 21.318 36.791 69.261 1.00 13.08 O
ANISOU 2389 O ASP A 308 1503 1636 1829 79 34 106 O
ATOM 2390 CB ASP A 308 18.006 36.406 68.840 1.00 12.96 C
ANISOU 2390 CB ASP A 308 1458 1636 1829 64 43 126 C
ATOM 2391 CG ASP A 308 18.226 36.000 70.280 1.00 15.13 C
ANISOU 2391 CG ASP A 308 1736 1913 2100 73 51 140 C
ATOM 2392 OD1 ASP A 308 18.479 36.860 71.114 1.00 14.99 O
ANISOU 2392 OD1 ASP A 308 1724 1904 2067 87 55 141 O
ATOM 2393 OD2 ASP A 308 18.256 34.783 70.528 1.00 21.02 O
ANISOU 2393 OD2 ASP A 308 2480 2650 2858 65 55 149 O
ATOM 2394 N ARG A 309 20.768 35.674 67.412 1.00 11.27 N
ANISOU 2394 N ARG A 309 1266 1393 1622 55 28 98 N
ATOM 2395 CA ARG A 309 21.972 34.833 67.349 1.00 11.24 C
ANISOU 2395 CA ARG A 309 1271 1376 1626 54 26 93 C
ATOM 2396 C ARG A 309 23.204 35.619 66.954 1.00 10.62 C
ANISOU 2396 C ARG A 309 1201 1297 1537 60 20 79 C
ATOM 2397 O ARG A 309 24.313 35.287 67.326 1.00 11.07 O
ANISOU 2397 O ARG A 309 1265 1348 1594 65 20 78 O
ATOM 2398 CB ARG A 309 21.725 33.715 66.398 1.00 11.76 C
ANISOU 2398 CB ARG A 309 1333 1427 1707 39 25 89 C
ATOM 2399 CG ARG A 309 20.705 32.728 66.938 1.00 13.28 C
ANISOU 2399 CG ARG A 309 1518 1617 1911 31 31 104 C
ATOM 2400 CD ARG A 309 20.349 31.670 65.903 1.00 15.10 C
ANISOU 2400 CD ARG A 309 1746 1834 2158 13 29 98 C
ATOM 2401 NE ARG A 309 19.309 30.740 66.408 1.00 18.29 N
ANISOU 2401 NE ARG A 309 2141 2234 2573 3 35 114 N
ATOM 2402 CZ ARG A 309 19.594 29.631 67.114 1.00 20.71 C
ANISOU 2402 CZ ARG A 309 2452 2527 2890 3 42 125 C
ATOM 2403 NH1 ARG A 309 20.858 29.328 67.415 1.00 20.96 N
ANISOU 2403 NH1 ARG A 309 2494 2548 2921 13 42 123 N
ATOM 2404 NH2 ARG A 309 18.604 28.809 67.514 1.00 24.60 N
ANISOU 2404 NH2 ARG A 309 2936 3016 3393 -8 48 139 N
ATOM 2405 N MET A 310 22.970 36.715 66.244 1.00 9.82 N
ANISOU 2405 N MET A 310 1100 1203 1427 60 15 70 N
ATOM 2406 CA MET A 310 24.088 37.601 65.797 1.00 9.81 C
ANISOU 2406 CA MET A 310 1108 1203 1418 64 10 57 C
ATOM 2407 C MET A 310 24.465 38.632 66.865 1.00 10.02 C
ANISOU 2407 C MET A 310 1139 1238 1428 78 11 60 C
ATOM 2408 O MET A 310 25.630 39.032 66.986 1.00 10.72 O
ANISOU 2408 O MET A 310 1236 1327 1511 82 8 53 O
ATOM 2409 CB MET A 310 23.783 38.350 64.507 1.00 10.21 C
ANISOU 2409 CB MET A 310 1158 1256 1466 58 4 45 C
ATOM 2410 CG MET A 310 23.581 37.390 63.343 1.00 11.04 C
ANISOU 2410 CG MET A 310 1260 1353 1584 44 1 39 C
ATOM 2411 SD MET A 310 23.137 38.415 61.894 1.00 15.41 S
ANISOU 2411 SD MET A 310 1811 1913 2130 39 -6 28 S
ATOM 2412 CE MET A 310 23.507 37.294 60.656 1.00 15.78 C
ANISOU 2412 CE MET A 310 1859 1948 2188 25 -10 16 C
ATOM 2413 N LEU A 311 23.492 39.045 67.628 1.00 9.95 N
ANISOU 2413 N LEU A 311 1127 1238 1414 83 16 69 N
ATOM 2414 CA LEU A 311 23.649 40.105 68.645 1.00 10.08 C
ANISOU 2414 CA LEU A 311 1150 1264 1415 96 19 71 C
ATOM 2415 C LEU A 311 23.717 39.517 70.031 1.00 12.03 C
ANISOU 2415 C LEU A 311 1397 1514 1659 103 25 84 C
ATOM 2416 O LEU A 311 23.052 39.993 70.953 1.00 14.18 O
ANISOU 2416 O LEU A 311 1669 1796 1922 112 31 91 O
ATOM 2417 CB LEU A 311 22.595 41.210 68.553 1.00 10.00 C
ANISOU 2417 CB LEU A 311 1138 1263 1398 101 21 71 C
ATOM 2418 CG LEU A 311 22.539 42.004 67.245 1.00 9.98 C
ANISOU 2418 CG LEU A 311 1137 1259 1396 96 15 60 C
ATOM 2419 CD1 LEU A 311 21.505 43.087 67.278 1.00 9.92 C
ANISOU 2419 CD1 LEU A 311 1128 1261 1381 104 18 62 C
ATOM 2420 CD2 LEU A 311 23.913 42.631 66.937 1.00 9.47 C
ANISOU 2420 CD2 LEU A 311 1084 1191 1325 96 8 47 C
ATOM 2421 N THR A 312 24.512 38.485 70.193 1.00 11.94 N
ANISOU 2421 N THR A 312 1386 1495 1654 100 24 86 N
ATOM 2422 CA THR A 312 24.826 37.947 71.551 1.00 11.97 C
ANISOU 2422 CA THR A 312 1392 1503 1655 108 29 99 C
ATOM 2423 C THR A 312 25.866 38.803 72.245 1.00 11.50 C
ANISOU 2423 C THR A 312 1341 1450 1578 117 25 94 C
ATOM 2424 O THR A 312 26.831 39.242 71.635 1.00 11.05 O
ANISOU 2424 O THR A 312 1289 1391 1519 115 18 81 O
ATOM 2425 CB THR A 312 25.296 36.485 71.511 1.00 13.91 C
ANISOU 2425 CB THR A 312 1634 1736 1913 104 30 106 C
ATOM 2426 OG1 THR A 312 26.603 36.402 70.844 1.00 14.79 O
ANISOU 2426 OG1 THR A 312 1751 1841 2028 102 22 94 O
ATOM 2427 CG2 THR A 312 24.214 35.693 70.796 1.00 13.98 C
ANISOU 2427 CG2 THR A 312 1635 1738 1939 93 33 110 C
ATOM 2428 N PHE A 313 25.697 39.034 73.540 1.00 10.95 N
ANISOU 2428 N PHE A 313 1274 1391 1496 127 30 103 N
ATOM 2429 CA PHE A 313 26.679 39.788 74.289 1.00 11.51 C
ANISOU 2429 CA PHE A 313 1354 1470 1550 134 25 97 C
ATOM 2430 C PHE A 313 28.044 39.098 74.293 1.00 11.68 C
ANISOU 2430 C PHE A 313 1375 1487 1575 133 19 97 C
ATOM 2431 O PHE A 313 29.050 39.732 74.048 1.00 12.96 O
ANISOU 2431 O PHE A 313 1542 1650 1730 132 12 85 O
ATOM 2432 CB PHE A 313 26.210 39.989 75.745 1.00 12.00 C
ANISOU 2432 CB PHE A 313 1418 1544 1597 144 32 108 C
ATOM 2433 CG PHE A 313 27.223 40.665 76.600 1.00 11.32 C
ANISOU 2433 CG PHE A 313 1341 1467 1493 150 27 103 C
ATOM 2434 CD1 PHE A 313 27.337 42.047 76.632 1.00 11.98 C
ANISOU 2434 CD1 PHE A 313 1434 1555 1562 153 24 89 C
ATOM 2435 CD2 PHE A 313 28.069 39.916 77.402 1.00 11.35 C
ANISOU 2435 CD2 PHE A 313 1344 1475 1493 154 25 112 C
ATOM 2436 CE1 PHE A 313 28.289 42.653 77.457 1.00 11.79 C
ANISOU 2436 CE1 PHE A 313 1419 1540 1521 156 19 83 C
ATOM 2437 CE2 PHE A 313 29.016 40.485 78.192 1.00 11.84 C
ANISOU 2437 CE2 PHE A 313 1414 1547 1537 158 19 107 C
ATOM 2438 CZ PHE A 313 29.142 41.851 78.241 1.00 12.06 C
ANISOU 2438 CZ PHE A 313 1451 1580 1551 159 15 93 C
ATOM 2439 N ASN A 314 28.037 37.795 74.524 1.00 11.05 N
ANISOU 2439 N ASN A 314 1291 1402 1507 132 23 110 N
ATOM 2440 CA ASN A 314 29.295 37.042 74.591 1.00 10.95 C
ANISOU 2440 CA ASN A 314 1277 1384 1497 134 18 112 C
ATOM 2441 C ASN A 314 29.725 36.645 73.181 1.00 10.39 C
ANISOU 2441 C ASN A 314 1205 1301 1443 125 14 101 C
ATOM 2442 O ASN A 314 29.010 35.929 72.505 1.00 10.31 O
ANISOU 2442 O ASN A 314 1190 1280 1448 119 18 103 O
ATOM 2443 CB ASN A 314 29.057 35.803 75.462 1.00 11.78 C
ANISOU 2443 CB ASN A 314 1378 1488 1608 139 25 132 C
ATOM 2444 CG ASN A 314 30.300 35.012 75.746 1.00 13.51 C
ANISOU 2444 CG ASN A 314 1597 1704 1830 144 21 137 C
ATOM 2445 OD1 ASN A 314 31.222 34.957 74.948 1.00 12.46 O
ANISOU 2445 OD1 ASN A 314 1465 1566 1704 141 15 127 O
ATOM 2446 ND2 ASN A 314 30.317 34.350 76.895 1.00 14.24 N
ANISOU 2446 ND2 ASN A 314 1690 1803 1919 152 25 155 N
ATOM 2447 N PRO A 315 30.908 37.112 72.752 1.00 9.52 N
ANISOU 2447 N PRO A 315 1096 1192 1328 125 7 89 N
ATOM 2448 CA PRO A 315 31.331 36.773 71.373 1.00 9.92 C
ANISOU 2448 CA PRO A 315 1145 1231 1393 117 4 78 C
ATOM 2449 C PRO A 315 31.518 35.297 71.151 1.00 10.45 C
ANISOU 2449 C PRO A 315 1208 1285 1476 117 8 86 C
ATOM 2450 O PRO A 315 31.444 34.872 70.002 1.00 10.55 O
ANISOU 2450 O PRO A 315 1220 1286 1501 110 8 78 O
ATOM 2451 CB PRO A 315 32.661 37.529 71.205 1.00 9.97 C
ANISOU 2451 CB PRO A 315 1154 1244 1390 118 -4 67 C
ATOM 2452 CG PRO A 315 33.140 37.762 72.629 1.00 10.37 C
ANISOU 2452 CG PRO A 315 1206 1308 1426 127 -6 76 C
ATOM 2453 CD PRO A 315 31.904 37.927 73.467 1.00 9.90 C
ANISOU 2453 CD PRO A 315 1149 1253 1360 130 0 85 C
ATOM 2454 N ASN A 316 31.812 34.534 72.202 1.00 10.84 N
ANISOU 2454 N ASN A 316 1257 1336 1526 125 11 101 N
ATOM 2455 CA ASN A 316 32.027 33.080 72.004 1.00 12.89 C
ANISOU 2455 CA ASN A 316 1515 1581 1803 126 15 110 C
ATOM 2456 C ASN A 316 30.726 32.375 71.639 1.00 13.80 C
ANISOU 2456 C ASN A 316 1629 1684 1932 118 22 115 C
ATOM 2457 O ASN A 316 30.745 31.260 71.101 1.00 16.90 O
ANISOU 2457 O ASN A 316 2021 2060 2342 115 25 117 O
ATOM 2458 CB ASN A 316 32.598 32.444 73.258 1.00 13.32 C
ANISOU 2458 CB ASN A 316 1568 1640 1854 138 16 127 C
ATOM 2459 CG ASN A 316 33.887 33.106 73.734 1.00 14.80 C
ANISOU 2459 CG ASN A 316 1755 1843 2027 146 9 124 C
ATOM 2460 OD1 ASN A 316 34.022 33.527 74.920 1.00 19.61 O
ANISOU 2460 OD1 ASN A 316 2364 2466 2619 153 7 133 O
ATOM 2461 ND2 ASN A 316 34.789 33.190 72.892 1.00 13.09 N
ANISOU 2461 ND2 ASN A 316 1537 1623 1814 144 4 113 N
ATOM 2462 N LYS A 317 29.605 32.947 72.037 1.00 12.63 N
ANISOU 2462 N LYS A 317 1479 1543 1777 116 25 118 N
ATOM 2463 CA LYS A 317 28.281 32.385 71.796 1.00 12.38 C
ANISOU 2463 CA LYS A 317 1444 1503 1756 107 31 125 C
ATOM 2464 C LYS A 317 27.619 32.882 70.533 1.00 12.25 C
ANISOU 2464 C LYS A 317 1426 1484 1744 95 28 110 C
ATOM 2465 O LYS A 317 26.540 32.393 70.124 1.00 12.76 O
ANISOU 2465 O LYS A 317 1487 1542 1820 86 32 112 O
ATOM 2466 CB LYS A 317 27.409 32.731 73.009 1.00 13.01 C
ANISOU 2466 CB LYS A 317 1522 1596 1825 112 36 139 C
ATOM 2467 CG LYS A 317 27.928 32.062 74.291 1.00 15.03 C
ANISOU 2467 CG LYS A 317 1778 1854 2076 123 40 157 C
ATOM 2468 CD LYS A 317 27.149 32.494 75.515 1.00 15.60 C
ANISOU 2468 CD LYS A 317 1851 1943 2135 129 45 170 C
ATOM 2469 CE LYS A 317 27.697 31.789 76.742 1.00 17.11 C
ANISOU 2469 CE LYS A 317 2043 2137 2322 139 48 188 C
ATOM 2470 NZ LYS A 317 26.923 32.249 77.917 1.00 18.10 N
ANISOU 2470 NZ LYS A 317 2167 2279 2431 145 54 200 N
ATOM 2471 N ARG A 318 28.314 33.743 69.832 1.00 10.79 N
ANISOU 2471 N ARG A 318 1244 1303 1552 95 21 94 N
ATOM 2472 CA ARG A 318 27.731 34.408 68.655 1.00 10.43 C
ANISOU 2472 CA ARG A 318 1198 1258 1508 86 18 80 C
ATOM 2473 C ARG A 318 27.801 33.495 67.450 1.00 10.16 C
ANISOU 2473 C ARG A 318 1163 1209 1489 76 17 72 C
ATOM 2474 O ARG A 318 28.800 32.763 67.276 1.00 11.44 O
ANISOU 2474 O ARG A 318 1327 1360 1657 78 17 70 O
ATOM 2475 CB ARG A 318 28.487 35.724 68.428 1.00 10.58 C
ANISOU 2475 CB ARG A 318 1221 1287 1512 89 12 68 C
ATOM 2476 CG ARG A 318 27.795 36.796 67.674 1.00 10.42 C
ANISOU 2476 CG ARG A 318 1200 1271 1486 84 9 59 C
ATOM 2477 CD ARG A 318 28.510 38.142 67.695 1.00 9.98 C
ANISOU 2477 CD ARG A 318 1151 1226 1416 89 4 49 C
ATOM 2478 NE ARG A 318 28.534 38.719 69.021 1.00 9.70 N
ANISOU 2478 NE ARG A 318 1118 1201 1368 98 5 57 N
ATOM 2479 CZ ARG A 318 29.518 39.467 69.549 1.00 9.20 C
ANISOU 2479 CZ ARG A 318 1060 1144 1292 103 1 52 C
ATOM 2480 NH1 ARG A 318 30.580 39.749 68.806 1.00 9.55 N
ANISOU 2480 NH1 ARG A 318 1106 1186 1336 99 -5 41 N
ATOM 2481 NH2 ARG A 318 29.461 39.879 70.820 1.00 8.72 N
ANISOU 2481 NH2 ARG A 318 1003 1093 1219 111 3 59 N
ATOM 2482 N ILE A 319 26.789 33.542 66.589 1.00 9.75 N
ANISOU 2482 N ILE A 319 1108 1154 1442 65 17 67 N
ATOM 2483 CA ILE A 319 26.714 32.674 65.428 1.00 9.68 C
ANISOU 2483 CA ILE A 319 1100 1132 1448 53 16 58 C
ATOM 2484 C ILE A 319 27.875 32.925 64.476 1.00 9.69 C
ANISOU 2484 C ILE A 319 1106 1130 1447 54 11 42 C
ATOM 2485 O ILE A 319 28.326 34.077 64.329 1.00 9.75 O
ANISOU 2485 O ILE A 319 1115 1149 1442 58 7 35 O
ATOM 2486 CB ILE A 319 25.327 32.803 64.756 1.00 9.89 C
ANISOU 2486 CB ILE A 319 1120 1160 1477 41 15 56 C
ATOM 2487 CG1 ILE A 319 25.016 31.692 63.764 1.00 10.02 C
ANISOU 2487 CG1 ILE A 319 1137 1162 1509 27 15 49 C
ATOM 2488 CG2 ILE A 319 25.199 34.172 64.123 1.00 9.97 C
ANISOU 2488 CG2 ILE A 319 1130 1184 1475 41 9 46 C
ATOM 2489 CD1 ILE A 319 23.567 31.675 63.383 1.00 10.44 C
ANISOU 2489 CD1 ILE A 319 1181 1219 1566 14 14 52 C
ATOM 2490 N THR A 320 28.338 31.899 63.796 1.00 9.34 N
ANISOU 2490 N THR A 320 1065 1071 1414 50 13 36 N
ATOM 2491 CA THR A 320 29.360 32.045 62.752 1.00 9.98 C
ANISOU 2491 CA THR A 320 1150 1149 1494 50 10 20 C
ATOM 2492 C THR A 320 28.714 32.342 61.398 1.00 9.55 C
ANISOU 2492 C THR A 320 1095 1096 1439 37 5 6 C
ATOM 2493 O THR A 320 27.546 32.159 61.230 1.00 9.33 O
ANISOU 2493 O THR A 320 1064 1067 1415 27 5 9 O
ATOM 2494 CB THR A 320 30.195 30.755 62.569 1.00 10.75 C
ANISOU 2494 CB THR A 320 1251 1230 1604 52 14 18 C
ATOM 2495 OG1 THR A 320 29.341 29.742 62.011 1.00 11.30 O
ANISOU 2495 OG1 THR A 320 1322 1284 1687 40 17 16 O
ATOM 2496 CG2 THR A 320 30.853 30.312 63.887 1.00 11.44 C
ANISOU 2496 CG2 THR A 320 1338 1316 1693 66 18 34 C
ATOM 2497 N VAL A 321 29.498 32.795 60.422 1.00 9.63 N
ANISOU 2497 N VAL A 321 1108 1108 1443 36 2 -8 N
ATOM 2498 CA VAL A 321 28.958 33.075 59.124 1.00 10.21 C
ANISOU 2498 CA VAL A 321 1181 1183 1514 24 -2 -20 C
ATOM 2499 C VAL A 321 28.317 31.867 58.430 1.00 10.49 C
ANISOU 2499 C VAL A 321 1219 1205 1563 12 0 -26 C
ATOM 2500 O VAL A 321 27.245 32.009 57.834 1.00 10.77 O
ANISOU 2500 O VAL A 321 1250 1243 1597 1 -4 -29 O
ATOM 2501 CB VAL A 321 30.001 33.807 58.214 1.00 10.24 C
ANISOU 2501 CB VAL A 321 1188 1192 1508 26 -5 -34 C
ATOM 2502 CG1 VAL A 321 31.195 32.885 57.841 1.00 10.25 C
ANISOU 2502 CG1 VAL A 321 1195 1183 1518 31 -1 -41 C
ATOM 2503 CG2 VAL A 321 29.326 34.388 57.016 1.00 10.42 C
ANISOU 2503 CG2 VAL A 321 1211 1222 1526 16 -10 -44 C
ATOM 2504 N GLU A 322 28.933 30.697 58.537 1.00 11.03 N
ANISOU 2504 N GLU A 322 1291 1256 1643 15 5 -27 N
ATOM 2505 CA GLU A 322 28.379 29.511 57.900 1.00 11.55 C
ANISOU 2505 CA GLU A 322 1361 1306 1722 3 7 -33 C
ATOM 2506 C GLU A 322 27.065 29.134 58.547 1.00 11.76 C
ANISOU 2506 C GLU A 322 1382 1330 1755 -6 8 -20 C
ATOM 2507 O GLU A 322 26.135 28.633 57.873 1.00 11.56 O
ANISOU 2507 O GLU A 322 1356 1300 1736 -22 6 -26 O
ATOM 2508 CB GLU A 322 29.344 28.347 57.985 1.00 12.64 C
ANISOU 2508 CB GLU A 322 1507 1425 1872 10 14 -35 C
ATOM 2509 CG GLU A 322 30.583 28.536 57.137 1.00 15.36 C
ANISOU 2509 CG GLU A 322 1855 1770 2210 16 15 -50 C
ATOM 2510 CD GLU A 322 31.678 29.325 57.801 1.00 16.95 C
ANISOU 2510 CD GLU A 322 2054 1984 2403 32 15 -43 C
ATOM 2511 OE1 GLU A 322 31.614 29.656 59.093 1.00 15.47 O
ANISOU 2511 OE1 GLU A 322 1862 1804 2214 40 15 -27 O
ATOM 2512 OE2 GLU A 322 32.621 29.601 56.963 1.00 20.88 O
ANISOU 2512 OE2 GLU A 322 2554 2486 2896 35 15 -56 O
ATOM 2513 N GLU A 323 27.014 29.248 59.858 1.00 11.21 N
ANISOU 2513 N GLU A 323 1308 1264 1685 4 11 -3 N
ATOM 2514 CA GLU A 323 25.759 28.922 60.579 1.00 11.99 C
ANISOU 2514 CA GLU A 323 1401 1363 1790 -3 13 11 C
ATOM 2515 C GLU A 323 24.655 29.892 60.180 1.00 11.54 C
ANISOU 2515 C GLU A 323 1335 1324 1724 -12 7 10 C
ATOM 2516 O GLU A 323 23.497 29.478 59.986 1.00 11.69 O
ANISOU 2516 O GLU A 323 1349 1342 1751 -25 6 13 O
ATOM 2517 CB GLU A 323 25.991 28.939 62.092 1.00 13.55 C
ANISOU 2517 CB GLU A 323 1597 1564 1987 10 18 30 C
ATOM 2518 CG GLU A 323 26.791 27.739 62.641 1.00 15.95 C
ANISOU 2518 CG GLU A 323 1907 1849 2303 17 25 37 C
ATOM 2519 CD GLU A 323 27.515 28.017 64.001 1.00 19.06 C
ANISOU 2519 CD GLU A 323 2300 2250 2690 35 28 52 C
ATOM 2520 OE1 GLU A 323 27.381 29.114 64.697 1.00 16.03 O
ANISOU 2520 OE1 GLU A 323 1912 1887 2293 42 26 59 O
ATOM 2521 OE2 GLU A 323 28.283 27.057 64.408 1.00 24.28 O
ANISOU 2521 OE2 GLU A 323 2966 2897 3361 43 34 58 O
ATOM 2522 N ALA A 324 25.016 31.156 60.021 1.00 10.31 N
ANISOU 2522 N ALA A 324 1180 1184 1555 -4 3 6 N
ATOM 2523 CA ALA A 324 24.054 32.184 59.708 1.00 9.74 C
ANISOU 2523 CA ALA A 324 1100 1128 1472 -8 -3 6 C
ATOM 2524 C ALA A 324 23.505 31.913 58.307 1.00 9.75 C
ANISOU 2524 C ALA A 324 1100 1127 1476 -24 -8 -7 C
ATOM 2525 O ALA A 324 22.284 31.967 58.067 1.00 9.20 O
ANISOU 2525 O ALA A 324 1022 1066 1408 -35 -12 -4 O
ATOM 2526 CB ALA A 324 24.678 33.547 59.860 1.00 9.83 C
ANISOU 2526 CB ALA A 324 1113 1153 1469 4 -5 5 C
ATOM 2527 N LEU A 325 24.381 31.558 57.364 1.00 9.42 N
ANISOU 2527 N LEU A 325 1066 1077 1435 -27 -10 -23 N
ATOM 2528 CA LEU A 325 23.889 31.195 56.025 1.00 9.77 C
ANISOU 2528 CA LEU A 325 1111 1120 1480 -43 -15 -37 C
ATOM 2529 C LEU A 325 22.883 30.055 56.010 1.00 10.18 C
ANISOU 2529 C LEU A 325 1160 1161 1546 -58 -15 -34 C
ATOM 2530 O LEU A 325 21.927 30.089 55.220 1.00 11.11 O
ANISOU 2530 O LEU A 325 1272 1286 1662 -73 -21 -40 O
ATOM 2531 CB LEU A 325 25.058 30.852 55.104 1.00 10.17 C
ANISOU 2531 CB LEU A 325 1173 1161 1530 -42 -15 -54 C
ATOM 2532 CG LEU A 325 25.862 32.084 54.607 1.00 10.17 C
ANISOU 2532 CG LEU A 325 1174 1174 1514 -32 -18 -60 C
ATOM 2533 CD1 LEU A 325 27.227 31.740 54.035 1.00 9.94 C
ANISOU 2533 CD1 LEU A 325 1154 1136 1485 -27 -14 -73 C
ATOM 2534 CD2 LEU A 325 25.077 32.903 53.560 1.00 10.59 C
ANISOU 2534 CD2 LEU A 325 1224 1244 1557 -42 -26 -66 C
ATOM 2535 N ALA A 326 23.077 29.122 56.919 1.00 10.63 N
ANISOU 2535 N ALA A 326 1219 1203 1615 -56 -7 -25 N
ATOM 2536 CA ALA A 326 22.206 27.982 57.012 1.00 10.96 C
ANISOU 2536 CA ALA A 326 1260 1233 1673 -71 -5 -22 C
ATOM 2537 C ALA A 326 20.934 28.225 57.817 1.00 10.65 C
ANISOU 2537 C ALA A 326 1207 1205 1635 -75 -5 -4 C
ATOM 2538 O ALA A 326 20.116 27.315 57.972 1.00 11.98 O
ANISOU 2538 O ALA A 326 1372 1365 1816 -90 -3 2 O
ATOM 2539 CB ALA A 326 22.978 26.816 57.586 1.00 10.79 C
ANISOU 2539 CB ALA A 326 1248 1187 1664 -66 4 -19 C
ATOM 2540 N HIS A 327 20.746 29.421 58.351 1.00 10.72 N
ANISOU 2540 N HIS A 327 1209 1234 1632 -63 -6 6 N
ATOM 2541 CA HIS A 327 19.606 29.693 59.188 1.00 10.66 C
ANISOU 2541 CA HIS A 327 1188 1238 1625 -64 -4 23 C
ATOM 2542 C HIS A 327 18.317 29.663 58.358 1.00 10.91 C
ANISOU 2542 C HIS A 327 1208 1279 1657 -83 -11 20 C
ATOM 2543 O HIS A 327 18.323 30.139 57.250 1.00 10.65 O
ANISOU 2543 O HIS A 327 1176 1254 1617 -88 -19 7 O
ATOM 2544 CB HIS A 327 19.779 31.055 59.835 1.00 10.65 C
ANISOU 2544 CB HIS A 327 1183 1254 1608 -46 -4 30 C
ATOM 2545 CG HIS A 327 18.748 31.355 60.863 1.00 10.68 C
ANISOU 2545 CG HIS A 327 1175 1270 1611 -43 1 49 C
ATOM 2546 ND1 HIS A 327 17.507 31.836 60.514 1.00 10.74 N
ANISOU 2546 ND1 HIS A 327 1170 1295 1617 -50 -3 53 N
ATOM 2547 CD2 HIS A 327 18.750 31.244 62.216 1.00 10.65 C
ANISOU 2547 CD2 HIS A 327 1171 1267 1609 -32 9 65 C
ATOM 2548 CE1 HIS A 327 16.783 32.013 61.604 1.00 11.18 C
ANISOU 2548 CE1 HIS A 327 1216 1359 1672 -44 3 71 C
ATOM 2549 NE2 HIS A 327 17.505 31.651 62.649 1.00 10.51 N
ANISOU 2549 NE2 HIS A 327 1140 1265 1590 -34 11 78 N
ATOM 2550 N PRO A 328 17.193 29.186 58.918 1.00 11.69 N
ANISOU 2550 N PRO A 328 1296 1381 1765 -93 -9 34 N
ATOM 2551 CA PRO A 328 15.930 29.136 58.171 1.00 11.79 C
ANISOU 2551 CA PRO A 328 1296 1406 1780 -112 -16 32 C
ATOM 2552 C PRO A 328 15.510 30.434 57.476 1.00 11.42 C
ANISOU 2552 C PRO A 328 1240 1382 1718 -107 -24 29 C
ATOM 2553 O PRO A 328 14.884 30.382 56.397 1.00 11.65 O
ANISOU 2553 O PRO A 328 1262 1418 1745 -123 -34 20 O
ATOM 2554 CB PRO A 328 14.946 28.736 59.245 1.00 12.37 C
ANISOU 2554 CB PRO A 328 1356 1482 1862 -116 -9 53 C
ATOM 2555 CG PRO A 328 15.731 27.821 60.113 1.00 12.65 C
ANISOU 2555 CG PRO A 328 1403 1495 1907 -110 1 59 C
ATOM 2556 CD PRO A 328 17.106 28.461 60.185 1.00 11.74 C
ANISOU 2556 CD PRO A 328 1301 1377 1782 -90 2 51 C
ATOM 2557 N TYR A 329 15.815 31.600 58.056 1.00 10.93 N
ANISOU 2557 N TYR A 329 1177 1331 1643 -87 -22 36 N
ATOM 2558 CA TYR A 329 15.435 32.825 57.392 1.00 10.34 C
ANISOU 2558 CA TYR A 329 1097 1277 1556 -81 -29 33 C
ATOM 2559 C TYR A 329 15.918 32.887 55.960 1.00 10.23 C
ANISOU 2559 C TYR A 329 1091 1262 1536 -90 -38 14 C
ATOM 2560 O TYR A 329 15.204 33.443 55.084 1.00 9.74 O
ANISOU 2560 O TYR A 329 1019 1215 1466 -96 -47 11 O
ATOM 2561 CB TYR A 329 15.940 34.024 58.188 1.00 10.29 C
ANISOU 2561 CB TYR A 329 1094 1279 1538 -58 -24 40 C
ATOM 2562 CG TYR A 329 15.478 35.403 57.642 1.00 10.29 C
ANISOU 2562 CG TYR A 329 1088 1298 1524 -50 -30 40 C
ATOM 2563 CD1 TYR A 329 14.145 35.653 57.345 1.00 10.34 C
ANISOU 2563 CD1 TYR A 329 1077 1322 1530 -56 -34 48 C
ATOM 2564 CD2 TYR A 329 16.373 36.515 57.493 1.00 10.14 C
ANISOU 2564 CD2 TYR A 329 1079 1280 1492 -34 -31 34 C
ATOM 2565 CE1 TYR A 329 13.734 36.887 56.856 1.00 10.29 C
ANISOU 2565 CE1 TYR A 329 1065 1332 1511 -47 -39 50 C
ATOM 2566 CE2 TYR A 329 15.952 37.755 57.029 1.00 10.73 C
ANISOU 2566 CE2 TYR A 329 1150 1371 1555 -26 -35 35 C
ATOM 2567 CZ TYR A 329 14.648 37.948 56.716 1.00 10.46 C
ANISOU 2567 CZ TYR A 329 1100 1353 1522 -31 -39 43 C
ATOM 2568 OH TYR A 329 14.228 39.149 56.273 1.00 11.38 O
ANISOU 2568 OH TYR A 329 1212 1485 1628 -22 -43 46 O
ATOM 2569 N LEU A 330 17.126 32.388 55.690 1.00 9.96 N
ANISOU 2569 N LEU A 330 1071 1209 1503 -88 -37 1 N
ATOM 2570 CA LEU A 330 17.765 32.496 54.397 1.00 10.51 C
ANISOU 2570 CA LEU A 330 1150 1277 1565 -93 -43 -18 C
ATOM 2571 C LEU A 330 17.528 31.345 53.423 1.00 10.68 C
ANISOU 2571 C LEU A 330 1175 1289 1595 -115 -48 -32 C
ATOM 2572 O LEU A 330 18.181 31.254 52.406 1.00 10.48 O
ANISOU 2572 O LEU A 330 1159 1259 1564 -119 -52 -49 O
ATOM 2573 CB LEU A 330 19.259 32.680 54.615 1.00 10.99 C
ANISOU 2573 CB LEU A 330 1226 1327 1623 -79 -38 -24 C
ATOM 2574 CG LEU A 330 19.580 33.962 55.423 1.00 11.88 C
ANISOU 2574 CG LEU A 330 1338 1451 1726 -58 -35 -14 C
ATOM 2575 CD1 LEU A 330 21.050 34.029 55.729 1.00 12.47 C
ANISOU 2575 CD1 LEU A 330 1426 1515 1798 -46 -30 -19 C
ATOM 2576 CD2 LEU A 330 19.127 35.224 54.693 1.00 12.24 C
ANISOU 2576 CD2 LEU A 330 1378 1515 1757 -55 -42 -15 C
ATOM 2577 N GLU A 331 16.544 30.497 53.716 1.00 11.47 N
ANISOU 2577 N GLU A 331 1265 1385 1706 -130 -48 -25 N
ATOM 2578 CA GLU A 331 16.402 29.239 53.004 1.00 12.67 C
ANISOU 2578 CA GLU A 331 1422 1522 1868 -152 -51 -38 C
ATOM 2579 C GLU A 331 16.139 29.356 51.524 1.00 12.06 C
ANISOU 2579 C GLU A 331 1345 1454 1782 -166 -63 -55 C
ATOM 2580 O GLU A 331 16.480 28.437 50.802 1.00 12.74 O
ANISOU 2580 O GLU A 331 1442 1525 1872 -180 -64 -72 O
ATOM 2581 CB GLU A 331 15.335 28.364 53.679 1.00 14.87 C
ANISOU 2581 CB GLU A 331 1691 1797 2163 -167 -49 -26 C
ATOM 2582 CG GLU A 331 13.941 28.912 53.594 1.00 18.09 C
ANISOU 2582 CG GLU A 331 2078 2230 2567 -175 -56 -15 C
ATOM 2583 CD GLU A 331 13.169 28.522 52.354 1.00 22.00 C
ANISOU 2583 CD GLU A 331 2567 2732 3061 -200 -68 -27 C
ATOM 2584 OE1 GLU A 331 13.506 27.473 51.761 1.00 24.27 O
ANISOU 2584 OE1 GLU A 331 2866 3000 3356 -216 -69 -43 O
ATOM 2585 OE2 GLU A 331 12.218 29.277 51.997 1.00 26.77 O
ANISOU 2585 OE2 GLU A 331 3153 3361 3656 -203 -76 -21 O
ATOM 2586 N GLN A 332 15.523 30.433 51.030 1.00 11.72 N
ANISOU 2586 N GLN A 332 1290 1436 1725 -164 -71 -52 N
ATOM 2587 CA GLN A 332 15.307 30.550 49.603 1.00 12.03 C
ANISOU 2587 CA GLN A 332 1331 1487 1754 -177 -83 -67 C
ATOM 2588 C GLN A 332 16.633 30.639 48.855 1.00 11.78 C
ANISOU 2588 C GLN A 332 1317 1445 1713 -170 -82 -85 C
ATOM 2589 O GLN A 332 16.720 30.222 47.710 1.00 11.90 O
ANISOU 2589 O GLN A 332 1339 1459 1724 -183 -88 -103 O
ATOM 2590 CB GLN A 332 14.445 31.802 49.276 1.00 12.43 C
ANISOU 2590 CB GLN A 332 1365 1567 1792 -172 -92 -57 C
ATOM 2591 CG GLN A 332 14.010 31.997 47.801 1.00 13.69 C
ANISOU 2591 CG GLN A 332 1522 1743 1938 -186 -106 -70 C
ATOM 2592 CD GLN A 332 13.093 30.907 47.273 1.00 15.10 C
ANISOU 2592 CD GLN A 332 1692 1921 2123 -214 -114 -77 C
ATOM 2593 OE1 GLN A 332 13.567 29.837 46.899 1.00 17.53 O
ANISOU 2593 OE1 GLN A 332 2014 2208 2437 -228 -112 -94 O
ATOM 2594 NE2 GLN A 332 11.785 31.176 47.193 1.00 13.72 N
ANISOU 2594 NE2 GLN A 332 1497 1768 1948 -224 -122 -66 N
ATOM 2595 N TYR A 333 17.654 31.236 49.500 1.00 11.01 N
ANISOU 2595 N TYR A 333 1228 1343 1614 -148 -73 -80 N
ATOM 2596 CA TYR A 333 18.885 31.582 48.799 1.00 10.98 C
ANISOU 2596 CA TYR A 333 1237 1335 1599 -139 -72 -94 C
ATOM 2597 C TYR A 333 20.045 30.639 49.153 1.00 11.29 C
ANISOU 2597 C TYR A 333 1292 1349 1649 -134 -62 -102 C
ATOM 2598 O TYR A 333 20.992 30.516 48.385 1.00 11.05 O
ANISOU 2598 O TYR A 333 1273 1312 1613 -132 -61 -118 O
ATOM 2599 CB TYR A 333 19.281 33.060 49.095 1.00 10.43 C
ANISOU 2599 CB TYR A 333 1166 1281 1518 -119 -71 -84 C
ATOM 2600 CG TYR A 333 18.105 33.965 49.007 1.00 9.78 C
ANISOU 2600 CG TYR A 333 1068 1220 1428 -119 -79 -72 C
ATOM 2601 CD1 TYR A 333 17.420 34.093 47.781 1.00 10.17 C
ANISOU 2601 CD1 TYR A 333 1111 1284 1467 -133 -90 -79 C
ATOM 2602 CD2 TYR A 333 17.604 34.603 50.108 1.00 9.94 C
ANISOU 2602 CD2 TYR A 333 1078 1247 1450 -107 -75 -53 C
ATOM 2603 CE1 TYR A 333 16.286 34.874 47.680 1.00 9.98 C
ANISOU 2603 CE1 TYR A 333 1072 1283 1437 -133 -97 -67 C
ATOM 2604 CE2 TYR A 333 16.489 35.374 50.002 1.00 9.97 C
ANISOU 2604 CE2 TYR A 333 1068 1272 1448 -107 -81 -42 C
ATOM 2605 CZ TYR A 333 15.790 35.493 48.820 1.00 10.15 C
ANISOU 2605 CZ TYR A 333 1084 1310 1463 -120 -92 -48 C
ATOM 2606 OH TYR A 333 14.592 36.217 48.711 1.00 9.99 O
ANISOU 2606 OH TYR A 333 1046 1311 1437 -119 -99 -35 O
ATOM 2607 N TYR A 334 19.964 29.980 50.311 1.00 11.33 N
ANISOU 2607 N TYR A 334 1296 1340 1669 -132 -54 -91 N
ATOM 2608 CA TYR A 334 21.082 29.200 50.800 1.00 11.66 C
ANISOU 2608 CA TYR A 334 1351 1360 1721 -123 -44 -95 C
ATOM 2609 C TYR A 334 21.450 28.075 49.820 1.00 12.44 C
ANISOU 2609 C TYR A 334 1462 1441 1825 -137 -44 -116 C
ATOM 2610 O TYR A 334 20.586 27.292 49.405 1.00 13.49 O
ANISOU 2610 O TYR A 334 1593 1568 1963 -157 -49 -122 O
ATOM 2611 CB TYR A 334 20.777 28.635 52.154 1.00 12.55 C
ANISOU 2611 CB TYR A 334 1459 1461 1848 -120 -37 -78 C
ATOM 2612 CG TYR A 334 21.871 27.811 52.782 1.00 12.45 C
ANISOU 2612 CG TYR A 334 1459 1426 1847 -110 -26 -79 C
ATOM 2613 CD1 TYR A 334 23.187 28.260 52.880 1.00 12.81 C
ANISOU 2613 CD1 TYR A 334 1512 1470 1885 -92 -22 -82 C
ATOM 2614 CD2 TYR A 334 21.580 26.540 53.289 1.00 12.83 C
ANISOU 2614 CD2 TYR A 334 1510 1454 1912 -119 -21 -75 C
ATOM 2615 CE1 TYR A 334 24.163 27.487 53.494 1.00 12.41 C
ANISOU 2615 CE1 TYR A 334 1470 1400 1845 -81 -13 -80 C
ATOM 2616 CE2 TYR A 334 22.554 25.764 53.891 1.00 13.52 C
ANISOU 2616 CE2 TYR A 334 1608 1520 2010 -108 -11 -73 C
ATOM 2617 CZ TYR A 334 23.823 26.252 54.010 1.00 13.59 C
ANISOU 2617 CZ TYR A 334 1622 1529 2011 -89 -7 -75 C
ATOM 2618 OH TYR A 334 24.813 25.556 54.648 1.00 14.12 O
ANISOU 2618 OH TYR A 334 1698 1579 2088 -76 2 -72 O
ATOM 2619 N ASP A 335 22.720 28.024 49.467 1.00 12.48 N
ANISOU 2619 N ASP A 335 1479 1437 1825 -126 -39 -127 N
ATOM 2620 CA ASP A 335 23.214 27.050 48.488 1.00 13.33 C
ANISOU 2620 CA ASP A 335 1600 1528 1935 -135 -37 -148 C
ATOM 2621 C ASP A 335 24.721 26.948 48.681 1.00 13.79 C
ANISOU 2621 C ASP A 335 1670 1576 1995 -115 -27 -153 C
ATOM 2622 O ASP A 335 25.475 27.676 48.084 1.00 12.33 O
ANISOU 2622 O ASP A 335 1487 1402 1797 -107 -27 -160 O
ATOM 2623 CB ASP A 335 22.889 27.503 47.058 1.00 14.89 C
ANISOU 2623 CB ASP A 335 1798 1742 2117 -146 -47 -164 C
ATOM 2624 CG ASP A 335 23.348 26.506 46.012 1.00 16.50 C
ANISOU 2624 CG ASP A 335 2017 1930 2321 -156 -45 -188 C
ATOM 2625 OD1 ASP A 335 23.905 25.486 46.415 1.00 17.13 O
ANISOU 2625 OD1 ASP A 335 2108 1986 2416 -153 -36 -192 O
ATOM 2626 OD2 ASP A 335 23.183 26.858 44.825 1.00 17.52 O
ANISOU 2626 OD2 ASP A 335 2148 2074 2435 -165 -53 -202 O
ATOM 2627 N PRO A 336 25.136 26.025 49.561 1.00 15.90 N
ANISOU 2627 N PRO A 336 1942 1821 2278 -109 -18 -146 N
ATOM 2628 CA PRO A 336 26.557 25.967 49.876 1.00 18.10 C
ANISOU 2628 CA PRO A 336 2228 2090 2558 -89 -8 -147 C
ATOM 2629 C PRO A 336 27.445 25.542 48.683 1.00 19.80 C
ANISOU 2629 C PRO A 336 2456 2298 2769 -88 -5 -170 C
ATOM 2630 O PRO A 336 28.635 25.839 48.700 1.00 24.28 O
ANISOU 2630 O PRO A 336 3026 2866 3331 -72 1 -171 O
ATOM 2631 CB PRO A 336 26.622 24.982 51.075 1.00 20.00 C
ANISOU 2631 CB PRO A 336 2472 2310 2819 -84 0 -134 C
ATOM 2632 CG PRO A 336 25.283 24.400 51.216 1.00 18.56 C
ANISOU 2632 CG PRO A 336 2285 2123 2646 -103 -4 -130 C
ATOM 2633 CD PRO A 336 24.310 25.144 50.395 1.00 17.56 C
ANISOU 2633 CD PRO A 336 2149 2016 2505 -118 -15 -135 C
ATOM 2634 N THR A 337 26.863 25.022 47.616 1.00 17.69 N
ANISOU 2634 N THR A 337 2195 2027 2499 -106 -9 -187 N
ATOM 2635 CA THR A 337 27.590 24.795 46.354 1.00 18.58 C
ANISOU 2635 CA THR A 337 2320 2138 2603 -107 -7 -210 C
ATOM 2636 C THR A 337 27.849 26.054 45.534 1.00 18.63 C
ANISOU 2636 C THR A 337 2320 2170 2587 -104 -13 -214 C
ATOM 2637 O THR A 337 28.569 26.024 44.506 1.00 18.79 O
ANISOU 2637 O THR A 337 2350 2193 2598 -102 -10 -231 O
ATOM 2638 CB THR A 337 26.888 23.754 45.448 1.00 19.44 C
ANISOU 2638 CB THR A 337 2438 2232 2715 -129 -10 -229 C
ATOM 2639 OG1 THR A 337 25.738 24.325 44.800 1.00 20.21 O
ANISOU 2639 OG1 THR A 337 2527 2350 2801 -147 -24 -232 O
ATOM 2640 CG2 THR A 337 26.529 22.517 46.261 1.00 22.61 C
ANISOU 2640 CG2 THR A 337 2845 2607 3140 -134 -4 -224 C
ATOM 2641 N ASP A 338 27.281 27.170 45.983 1.00 14.30 N
ANISOU 2641 N ASP A 338 1759 1642 2031 -103 -21 -198 N
ATOM 2642 CA ASP A 338 27.345 28.434 45.267 1.00 13.87 C
ANISOU 2642 CA ASP A 338 1700 1613 1958 -101 -27 -199 C
ATOM 2643 C ASP A 338 27.726 29.537 46.206 1.00 12.83 C
ANISOU 2643 C ASP A 338 1559 1493 1823 -85 -26 -180 C
ATOM 2644 O ASP A 338 27.300 30.687 46.033 1.00 12.82 O
ANISOU 2644 O ASP A 338 1550 1512 1810 -86 -33 -173 O
ATOM 2645 CB ASP A 338 25.984 28.786 44.640 1.00 14.81 C
ANISOU 2645 CB ASP A 338 1811 1747 2067 -120 -40 -200 C
ATOM 2646 CG ASP A 338 26.073 29.929 43.634 1.00 17.15 C
ANISOU 2646 CG ASP A 338 2105 2068 2342 -119 -47 -204 C
ATOM 2647 OD1 ASP A 338 27.092 30.041 42.923 1.00 17.94 O
ANISOU 2647 OD1 ASP A 338 2213 2169 2433 -113 -42 -216 O
ATOM 2648 OD2 ASP A 338 25.084 30.683 43.511 1.00 18.60 O
ANISOU 2648 OD2 ASP A 338 2278 2269 2518 -126 -57 -196 O
ATOM 2649 N GLU A 339 28.509 29.178 47.220 1.00 11.57 N
ANISOU 2649 N GLU A 339 1401 1320 1675 -71 -17 -172 N
ATOM 2650 CA GLU A 339 28.969 30.176 48.247 1.00 10.68 C
ANISOU 2650 CA GLU A 339 1280 1218 1560 -56 -16 -155 C
ATOM 2651 C GLU A 339 30.503 29.946 48.402 1.00 10.62 C
ANISOU 2651 C GLU A 339 1278 1202 1555 -40 -6 -158 C
ATOM 2652 O GLU A 339 30.950 29.263 49.340 1.00 10.39 O
ANISOU 2652 O GLU A 339 1250 1159 1539 -31 1 -151 O
ATOM 2653 CB GLU A 339 28.212 29.934 49.529 1.00 11.10 C
ANISOU 2653 CB GLU A 339 1327 1265 1626 -56 -16 -138 C
ATOM 2654 CG GLU A 339 26.766 30.391 49.374 1.00 11.07 C
ANISOU 2654 CG GLU A 339 1315 1274 1617 -69 -26 -132 C
ATOM 2655 CD GLU A 339 25.760 29.850 50.350 1.00 11.32 C
ANISOU 2655 CD GLU A 339 1340 1298 1661 -75 -26 -119 C
ATOM 2656 OE1 GLU A 339 26.104 29.160 51.326 1.00 12.45 O
ANISOU 2656 OE1 GLU A 339 1485 1427 1817 -68 -18 -111 O
ATOM 2657 OE2 GLU A 339 24.532 30.086 50.128 1.00 12.43 O
ANISOU 2657 OE2 GLU A 339 1473 1450 1800 -87 -33 -116 O
ATOM 2658 N PRO A 340 31.268 30.445 47.441 1.00 11.08 N
ANISOU 2658 N PRO A 340 1340 1270 1601 -38 -5 -169 N
ATOM 2659 CA PRO A 340 32.695 30.076 47.387 1.00 11.73 C
ANISOU 2659 CA PRO A 340 1427 1346 1685 -24 5 -175 C
ATOM 2660 C PRO A 340 33.556 30.663 48.493 1.00 11.66 C
ANISOU 2660 C PRO A 340 1411 1342 1679 -9 8 -159 C
ATOM 2661 O PRO A 340 33.161 31.626 49.181 1.00 11.25 O
ANISOU 2661 O PRO A 340 1352 1301 1622 -8 2 -146 O
ATOM 2662 CB PRO A 340 33.155 30.536 46.019 1.00 13.10 C
ANISOU 2662 CB PRO A 340 1604 1531 1843 -27 4 -190 C
ATOM 2663 CG PRO A 340 32.157 31.497 45.531 1.00 13.13 C
ANISOU 2663 CG PRO A 340 1604 1552 1835 -39 -6 -187 C
ATOM 2664 CD PRO A 340 30.871 31.279 46.308 1.00 11.70 C
ANISOU 2664 CD PRO A 340 1417 1366 1662 -47 -13 -177 C
ATOM 2665 N VAL A 341 34.675 30.008 48.700 1.00 11.44 N
ANISOU 2665 N VAL A 341 1385 1303 1657 4 17 -162 N
ATOM 2666 CA VAL A 341 35.694 30.395 49.645 1.00 11.43 C
ANISOU 2666 CA VAL A 341 1378 1307 1658 19 20 -149 C
ATOM 2667 C VAL A 341 36.981 30.793 48.941 1.00 11.82 C
ANISOU 2667 C VAL A 341 1427 1367 1699 27 25 -157 C
ATOM 2668 O VAL A 341 37.203 30.546 47.753 1.00 13.25 O
ANISOU 2668 O VAL A 341 1613 1547 1874 23 29 -173 O
ATOM 2669 CB VAL A 341 35.961 29.319 50.687 1.00 12.10 C
ANISOU 2669 CB VAL A 341 1464 1375 1760 29 26 -141 C
ATOM 2670 CG1 VAL A 341 34.705 29.034 51.499 1.00 12.99 C
ANISOU 2670 CG1 VAL A 341 1576 1480 1881 21 22 -130 C
ATOM 2671 CG2 VAL A 341 36.556 28.040 50.045 1.00 12.70 C
ANISOU 2671 CG2 VAL A 341 1548 1432 1845 34 36 -154 C
ATOM 2672 N ALA A 342 37.871 31.433 49.703 1.00 12.32 N
ANISOU 2672 N ALA A 342 1482 1440 1761 38 26 -146 N
ATOM 2673 CA ALA A 342 39.147 31.908 49.184 1.00 15.18 C
ANISOU 2673 CA ALA A 342 1839 1813 2114 45 31 -150 C
ATOM 2674 C ALA A 342 40.108 30.782 48.960 1.00 16.76 C
ANISOU 2674 C ALA A 342 2042 2002 2324 57 42 -157 C
ATOM 2675 O ALA A 342 40.042 29.825 49.651 1.00 16.22 O
ANISOU 2675 O ALA A 342 1977 1919 2269 64 45 -153 O
ATOM 2676 CB ALA A 342 39.750 32.941 50.146 1.00 14.73 C
ANISOU 2676 CB ALA A 342 1773 1770 2053 51 27 -136 C
ATOM 2677 N GLU A 343 41.051 31.035 48.063 1.00 19.64 N
ANISOU 2677 N GLU A 343 2405 2376 2680 60 47 -167 N
ATOM 2678 CA GLU A 343 42.161 30.094 47.738 1.00 24.70 C
ANISOU 2678 CA GLU A 343 3047 3010 3327 74 60 -174 C
ATOM 2679 C GLU A 343 42.973 29.718 48.988 1.00 21.64 C
ANISOU 2679 C GLU A 343 2651 2619 2951 91 63 -159 C
ATOM 2680 O GLU A 343 43.244 28.555 49.247 1.00 24.18 O
ANISOU 2680 O GLU A 343 2976 2924 3287 102 71 -159 O
ATOM 2681 CB GLU A 343 43.105 30.748 46.687 1.00 28.33 C
ANISOU 2681 CB GLU A 343 3504 3487 3774 75 65 -182 C
ATOM 2682 CG GLU A 343 42.491 31.060 45.314 1.00 33.73 C
ANISOU 2682 CG GLU A 343 4196 4177 4445 61 63 -198 C
ATOM 2683 CD GLU A 343 42.016 29.821 44.577 1.00 40.83 C
ANISOU 2683 CD GLU A 343 5108 5057 5348 60 69 -214 C
ATOM 2684 OE1 GLU A 343 42.832 28.917 44.370 1.00 49.10 O
ANISOU 2684 OE1 GLU A 343 6159 6095 6403 72 80 -222 O
ATOM 2685 OE2 GLU A 343 40.813 29.753 44.197 1.00 51.33 O
ANISOU 2685 OE2 GLU A 343 6446 6382 6675 45 62 -221 O
ATOM 2686 N GLU A 344 43.265 30.714 49.816 1.00 19.89 N
ANISOU 2686 N GLU A 344 2419 2413 2725 91 56 -145 N
ATOM 2687 CA GLU A 344 44.214 30.547 50.897 1.00 17.81 C
ANISOU 2687 CA GLU A 344 2145 2153 2469 106 58 -131 C
ATOM 2688 C GLU A 344 44.048 31.686 51.933 1.00 15.67 C
ANISOU 2688 C GLU A 344 1867 1896 2192 101 47 -117 C
ATOM 2689 O GLU A 344 43.793 32.826 51.541 1.00 16.44 O
ANISOU 2689 O GLU A 344 1963 2006 2276 89 41 -119 O
ATOM 2690 CB GLU A 344 45.610 30.662 50.283 1.00 17.66 C
ANISOU 2690 CB GLU A 344 2117 2146 2445 116 66 -136 C
ATOM 2691 CG GLU A 344 46.768 30.354 51.228 1.00 16.24 C
ANISOU 2691 CG GLU A 344 1926 1972 2274 133 69 -122 C
ATOM 2692 CD GLU A 344 48.091 30.203 50.510 1.00 15.72 C
ANISOU 2692 CD GLU A 344 1852 1916 2206 144 80 -128 C
ATOM 2693 OE1 GLU A 344 48.108 29.559 49.463 1.00 16.89 O
ANISOU 2693 OE1 GLU A 344 2008 2055 2355 147 89 -143 O
ATOM 2694 OE2 GLU A 344 49.119 30.622 51.061 1.00 13.42 O
ANISOU 2694 OE2 GLU A 344 1545 1640 1913 152 79 -118 O
ATOM 2695 N PRO A 345 44.356 31.388 53.219 1.00 14.49 N
ANISOU 2695 N PRO A 345 1710 1745 2049 112 45 -102 N
ATOM 2696 CA PRO A 345 44.330 32.532 54.101 1.00 14.09 C
ANISOU 2696 CA PRO A 345 1653 1710 1990 107 35 -91 C
ATOM 2697 C PRO A 345 45.456 33.508 53.867 1.00 12.44 C
ANISOU 2697 C PRO A 345 1434 1521 1771 106 34 -91 C
ATOM 2698 O PRO A 345 46.484 33.171 53.277 1.00 11.17 O
ANISOU 2698 O PRO A 345 1267 1365 1612 114 42 -95 O
ATOM 2699 CB PRO A 345 44.484 31.923 55.494 1.00 15.33 C
ANISOU 2699 CB PRO A 345 1806 1863 2157 119 34 -75 C
ATOM 2700 CG PRO A 345 44.034 30.517 55.345 1.00 17.55 C
ANISOU 2700 CG PRO A 345 2095 2121 2451 125 42 -78 C
ATOM 2701 CD PRO A 345 44.573 30.138 53.958 1.00 16.48 C
ANISOU 2701 CD PRO A 345 1963 1982 2316 126 51 -94 C
ATOM 2702 N PHE A 346 45.295 34.703 54.394 1.00 10.70 N
ANISOU 2702 N PHE A 346 1211 1314 1542 97 25 -85 N
ATOM 2703 CA PHE A 346 46.285 35.770 54.322 1.00 11.00 C
ANISOU 2703 CA PHE A 346 1238 1370 1569 94 22 -83 C
ATOM 2704 C PHE A 346 46.986 35.974 55.665 1.00 10.82 C
ANISOU 2704 C PHE A 346 1206 1359 1548 100 17 -70 C
ATOM 2705 O PHE A 346 46.466 35.590 56.710 1.00 11.09 O
ANISOU 2705 O PHE A 346 1242 1386 1585 105 13 -61 O
ATOM 2706 CB PHE A 346 45.666 37.118 53.901 1.00 11.28 C
ANISOU 2706 CB PHE A 346 1280 1413 1593 78 16 -87 C
ATOM 2707 CG PHE A 346 45.035 37.133 52.514 1.00 11.65 C
ANISOU 2707 CG PHE A 346 1336 1454 1636 69 19 -100 C
ATOM 2708 CD1 PHE A 346 45.371 36.197 51.535 1.00 12.75 C
ANISOU 2708 CD1 PHE A 346 1477 1589 1780 75 29 -109 C
ATOM 2709 CD2 PHE A 346 44.147 38.139 52.183 1.00 11.59 C
ANISOU 2709 CD2 PHE A 346 1335 1449 1619 57 13 -101 C
ATOM 2710 CE1 PHE A 346 44.771 36.254 50.288 1.00 13.56 C
ANISOU 2710 CE1 PHE A 346 1588 1688 1877 66 31 -121 C
ATOM 2711 CE2 PHE A 346 43.591 38.239 50.899 1.00 12.15 C
ANISOU 2711 CE2 PHE A 346 1413 1518 1685 49 16 -112 C
ATOM 2712 CZ PHE A 346 43.890 37.259 49.974 1.00 12.38 C
ANISOU 2712 CZ PHE A 346 1444 1542 1718 53 24 -122 C
ATOM 2713 N THR A 347 48.152 36.591 55.619 1.00 10.55 N
ANISOU 2713 N THR A 347 1160 1341 1507 100 16 -68 N
ATOM 2714 CA THR A 347 48.868 37.005 56.812 1.00 11.77 C
ANISOU 2714 CA THR A 347 1304 1510 1660 103 9 -57 C
ATOM 2715 C THR A 347 49.295 38.435 56.673 1.00 12.11 C
ANISOU 2715 C THR A 347 1343 1568 1690 88 2 -59 C
ATOM 2716 O THR A 347 49.751 38.890 55.613 1.00 12.04 O
ANISOU 2716 O THR A 347 1332 1565 1677 82 6 -66 O
ATOM 2717 CB THR A 347 50.029 36.062 57.102 1.00 12.98 C
ANISOU 2717 CB THR A 347 1444 1668 1820 119 14 -50 C
ATOM 2718 OG1 THR A 347 50.599 36.428 58.378 1.00 14.27 O
ANISOU 2718 OG1 THR A 347 1597 1846 1980 122 5 -38 O
ATOM 2719 CG2 THR A 347 51.075 36.176 55.995 1.00 13.83 C
ANISOU 2719 CG2 THR A 347 1543 1787 1927 120 21 -57 C
ATOM 2720 N PHE A 348 49.142 39.202 57.758 1.00 11.89 N
ANISOU 2720 N PHE A 348 1315 1546 1656 83 -8 -52 N
ATOM 2721 CA PHE A 348 49.653 40.569 57.903 1.00 12.95 C
ANISOU 2721 CA PHE A 348 1446 1695 1779 69 -15 -52 C
ATOM 2722 C PHE A 348 50.241 40.629 59.303 1.00 15.32 C
ANISOU 2722 C PHE A 348 1737 2006 2077 73 -23 -42 C
ATOM 2723 O PHE A 348 49.494 40.545 60.314 1.00 16.72 O
ANISOU 2723 O PHE A 348 1921 2178 2253 76 -29 -37 O
ATOM 2724 CB PHE A 348 48.549 41.610 57.804 1.00 13.06 C
ANISOU 2724 CB PHE A 348 1475 1702 1786 55 -20 -57 C
ATOM 2725 CG PHE A 348 47.931 41.731 56.461 1.00 11.53 C
ANISOU 2725 CG PHE A 348 1290 1500 1592 50 -14 -66 C
ATOM 2726 CD1 PHE A 348 48.650 42.228 55.400 1.00 11.95 C
ANISOU 2726 CD1 PHE A 348 1339 1561 1642 42 -10 -71 C
ATOM 2727 CD2 PHE A 348 46.592 41.418 56.271 1.00 11.57 C
ANISOU 2727 CD2 PHE A 348 1308 1490 1599 50 -13 -68 C
ATOM 2728 CE1 PHE A 348 48.058 42.341 54.146 1.00 11.20 C
ANISOU 2728 CE1 PHE A 348 1252 1459 1544 37 -5 -79 C
ATOM 2729 CE2 PHE A 348 46.009 41.516 55.046 1.00 11.08 C
ANISOU 2729 CE2 PHE A 348 1253 1422 1536 45 -8 -76 C
ATOM 2730 CZ PHE A 348 46.753 42.013 53.986 1.00 11.41 C
ANISOU 2730 CZ PHE A 348 1290 1471 1572 38 -5 -82 C
ATOM 2731 N ALA A 349 51.532 40.787 59.397 1.00 15.28 N
ANISOU 2731 N ALA A 349 1716 2018 2070 73 -25 -38 N
ATOM 2732 CA ALA A 349 52.201 40.848 60.702 1.00 17.05 C
ANISOU 2732 CA ALA A 349 1930 2257 2291 76 -34 -29 C
ATOM 2733 C ALA A 349 51.980 42.200 61.371 1.00 18.22 C
ANISOU 2733 C ALA A 349 2085 2412 2427 59 -45 -30 C
ATOM 2734 O ALA A 349 51.894 43.199 60.701 1.00 15.44 O
ANISOU 2734 O ALA A 349 1739 2059 2070 45 -45 -38 O
ATOM 2735 CB ALA A 349 53.689 40.632 60.496 1.00 18.08 C
ANISOU 2735 CB ALA A 349 2039 2406 2423 80 -32 -25 C
ATOM 2736 N MET A 350 51.907 42.205 62.711 1.00 25.26 N
ANISOU 2736 N MET A 350 3892 2934 2772 -1081 -556 163 N
ATOM 2737 CA AMET A 350 51.732 43.464 63.435 0.50 26.19 C
ANISOU 2737 CA AMET A 350 3866 3171 2913 -1065 -496 137 C
ATOM 2738 CA BMET A 350 51.812 43.424 63.528 0.50 26.71 C
ANISOU 2738 CA BMET A 350 3944 3225 2979 -1066 -504 140 C
ATOM 2739 C MET A 350 52.872 44.438 63.135 1.00 25.80 C
ANISOU 2739 C MET A 350 3710 3072 3019 -874 -487 126 C
ATOM 2740 O MET A 350 52.654 45.660 63.150 1.00 23.84 O
ANISOU 2740 O MET A 350 3328 2922 2808 -822 -419 96 O
ATOM 2741 CB AMET A 350 51.594 43.245 64.957 0.50 27.82 C
ANISOU 2741 CB AMET A 350 4170 3381 3019 -1203 -544 156 C
ATOM 2742 CB BMET A 350 52.029 43.072 65.017 0.50 29.40 C
ANISOU 2742 CB BMET A 350 4410 3517 3244 -1173 -578 167 C
ATOM 2743 CG AMET A 350 50.215 42.803 65.432 0.50 29.67 C
ANISOU 2743 CG AMET A 350 4439 3758 3077 -1425 -511 149 C
ATOM 2744 CG BMET A 350 50.942 42.237 65.676 0.50 31.96 C
ANISOU 2744 CG BMET A 350 4853 3905 3384 -1409 -590 181 C
ATOM 2745 SD AMET A 350 48.812 43.892 65.046 0.50 29.85 S
ANISOU 2745 SD AMET A 350 4227 4062 3055 -1439 -372 79 S
ATOM 2746 SD BMET A 350 51.398 41.690 67.345 0.50 35.90 S
ANISOU 2746 SD BMET A 350 5545 4301 3793 -1533 -699 222 S
ATOM 2747 CE AMET A 350 49.297 45.404 65.879 0.50 29.62 C
ANISOU 2747 CE AMET A 350 4077 4069 3108 -1302 -342 45 C
ATOM 2748 CE BMET A 350 52.451 40.282 66.982 0.50 35.71 C
ANISOU 2748 CE BMET A 350 5770 4011 3786 -1470 -851 270 C
ATOM 2749 N GLU A 351 54.058 43.922 62.834 1.00 24.96 N
ANISOU 2749 N GLU A 351 3666 2827 2990 -769 -558 144 N
ATOM 2750 CA GLU A 351 55.208 44.790 62.559 1.00 25.97 C
ANISOU 2750 CA GLU A 351 3686 2933 3250 -615 -552 132 C
ATOM 2751 C GLU A 351 55.037 45.662 61.279 1.00 22.39 C
ANISOU 2751 C GLU A 351 3089 2552 2866 -531 -458 103 C
ATOM 2752 O GLU A 351 55.640 46.721 61.149 1.00 22.67 O
ANISOU 2752 O GLU A 351 3026 2611 2978 -454 -429 91 O
ATOM 2753 CB GLU A 351 56.476 43.949 62.500 1.00 29.82 C
ANISOU 2753 CB GLU A 351 4255 3289 3786 -517 -652 145 C
ATOM 2754 CG GLU A 351 56.867 43.303 63.851 1.00 34.60 C
ANISOU 2754 CG GLU A 351 5005 3807 4334 -570 -763 173 C
ATOM 2755 CD GLU A 351 56.137 41.985 64.160 1.00 38.77 C
ANISOU 2755 CD GLU A 351 5742 4260 4730 -700 -828 199 C
ATOM 2756 OE1 GLU A 351 55.187 41.611 63.443 1.00 35.07 O
ANISOU 2756 OE1 GLU A 351 5294 3829 4203 -776 -778 196 O
ATOM 2757 OE2 GLU A 351 56.521 41.310 65.144 1.00 44.54 O
ANISOU 2757 OE2 GLU A 351 6629 4890 5403 -737 -937 224 O
ATOM 2758 N LEU A 352 54.108 45.288 60.403 1.00 19.68 N
ANISOU 2758 N LEU A 352 2745 2252 2478 -569 -413 94 N
ATOM 2759 CA LEU A 352 53.711 46.191 59.311 1.00 19.73 C
ANISOU 2759 CA LEU A 352 2630 2338 2528 -508 -327 65 C
ATOM 2760 C LEU A 352 53.217 47.508 59.834 1.00 19.70 C
ANISOU 2760 C LEU A 352 2538 2433 2514 -508 -278 41 C
ATOM 2761 O LEU A 352 53.455 48.534 59.221 1.00 20.05 O
ANISOU 2761 O LEU A 352 2505 2495 2617 -424 -238 23 O
ATOM 2762 CB LEU A 352 52.596 45.577 58.468 1.00 19.65 C
ANISOU 2762 CB LEU A 352 2635 2380 2449 -570 -291 57 C
ATOM 2763 CG LEU A 352 52.927 44.459 57.512 1.00 21.24 C
ANISOU 2763 CG LEU A 352 2919 2490 2661 -547 -322 70 C
ATOM 2764 CD1 LEU A 352 51.609 44.072 56.853 1.00 21.79 C
ANISOU 2764 CD1 LEU A 352 2993 2643 2643 -642 -279 62 C
ATOM 2765 CD2 LEU A 352 53.922 44.909 56.435 1.00 21.50 C
ANISOU 2765 CD2 LEU A 352 2879 2483 2808 -401 -299 57 C
ATOM 2766 N ASP A 353 52.554 47.481 60.999 1.00 20.95 N
ANISOU 2766 N ASP A 353 2725 2650 2586 -604 -287 38 N
ATOM 2767 CA ASP A 353 51.950 48.663 61.590 1.00 22.13 C
ANISOU 2767 CA ASP A 353 2802 2904 2701 -596 -245 3 C
ATOM 2768 C ASP A 353 52.983 49.623 62.133 1.00 22.40 C
ANISOU 2768 C ASP A 353 2827 2875 2808 -525 -267 9 C
ATOM 2769 O ASP A 353 52.659 50.755 62.442 1.00 23.91 O
ANISOU 2769 O ASP A 353 2977 3124 2984 -487 -239 -22 O
ATOM 2770 CB ASP A 353 51.002 48.267 62.734 1.00 23.32 C
ANISOU 2770 CB ASP A 353 2984 3153 2725 -731 -247 -7 C
ATOM 2771 CG ASP A 353 49.799 47.410 62.268 1.00 26.64 C
ANISOU 2771 CG ASP A 353 3402 3679 3042 -840 -218 -18 C
ATOM 2772 OD1 ASP A 353 49.699 47.050 61.077 1.00 30.18 O
ANISOU 2772 OD1 ASP A 353 3839 4108 3520 -807 -203 -15 O
ATOM 2773 OD2 ASP A 353 48.982 47.090 63.155 1.00 30.14 O
ANISOU 2773 OD2 ASP A 353 3859 4231 3362 -974 -213 -30 O
ATOM 2774 N ASP A 354 54.226 49.198 62.223 1.00 21.06 N
ANISOU 2774 N ASP A 354 2699 2595 2709 -501 -323 44 N
ATOM 2775 CA ASP A 354 55.264 50.070 62.743 1.00 23.41 C
ANISOU 2775 CA ASP A 354 2980 2848 3066 -455 -349 51 C
ATOM 2776 C ASP A 354 56.191 50.541 61.639 1.00 20.88 C
ANISOU 2776 C ASP A 354 2604 2494 2837 -369 -335 52 C
ATOM 2777 O ASP A 354 57.106 51.295 61.918 1.00 20.84 O
ANISOU 2777 O ASP A 354 2579 2465 2875 -348 -354 59 O
ATOM 2778 CB ASP A 354 56.072 49.357 63.833 1.00 27.45 C
ANISOU 2778 CB ASP A 354 3565 3287 3577 -496 -433 84 C
ATOM 2779 CG ASP A 354 55.199 48.867 65.000 1.00 31.64 C
ANISOU 2779 CG ASP A 354 4171 3850 4000 -610 -450 88 C
ATOM 2780 OD1 ASP A 354 54.239 49.583 65.372 1.00 37.90 O
ANISOU 2780 OD1 ASP A 354 4930 4741 4730 -643 -398 57 O
ATOM 2781 OD2 ASP A 354 55.474 47.744 65.532 1.00 36.21 O
ANISOU 2781 OD2 ASP A 354 4851 4359 4547 -665 -522 117 O
ATOM 2782 N LEU A 355 55.953 50.116 60.391 1.00 19.44 N
ANISOU 2782 N LEU A 355 2397 2317 2674 -335 -301 45 N
ATOM 2783 CA LEU A 355 56.831 50.546 59.289 1.00 18.22 C
ANISOU 2783 CA LEU A 355 2186 2144 2592 -268 -280 42 C
ATOM 2784 C LEU A 355 56.719 52.049 59.093 1.00 17.22 C
ANISOU 2784 C LEU A 355 2035 2044 2466 -253 -243 26 C
ATOM 2785 O LEU A 355 55.624 52.635 59.188 1.00 17.47 O
ANISOU 2785 O LEU A 355 2077 2118 2441 -252 -213 3 O
ATOM 2786 CB LEU A 355 56.521 49.826 57.987 1.00 18.02 C
ANISOU 2786 CB LEU A 355 2150 2119 2577 -238 -248 34 C
ATOM 2787 CG LEU A 355 56.961 48.408 57.776 1.00 20.06 C
ANISOU 2787 CG LEU A 355 2451 2325 2846 -222 -293 44 C
ATOM 2788 CD1 LEU A 355 56.420 47.912 56.437 1.00 20.49 C
ANISOU 2788 CD1 LEU A 355 2505 2387 2895 -201 -250 32 C
ATOM 2789 CD2 LEU A 355 58.477 48.338 57.827 1.00 21.83 C
ANISOU 2789 CD2 LEU A 355 2637 2521 3135 -159 -336 45 C
ATOM 2790 N PRO A 356 57.852 52.716 58.839 1.00 16.99 N
ANISOU 2790 N PRO A 356 1976 1995 2483 -242 -250 34 N
ATOM 2791 CA PRO A 356 57.718 54.119 58.494 1.00 16.24 C
ANISOU 2791 CA PRO A 356 1898 1903 2370 -239 -223 23 C
ATOM 2792 C PRO A 356 56.881 54.345 57.240 1.00 14.72 C
ANISOU 2792 C PRO A 356 1705 1726 2160 -200 -173 2 C
ATOM 2793 O PRO A 356 56.859 53.501 56.314 1.00 13.15 O
ANISOU 2793 O PRO A 356 1473 1537 1988 -182 -150 2 O
ATOM 2794 CB PRO A 356 59.154 54.597 58.257 1.00 18.45 C
ANISOU 2794 CB PRO A 356 2145 2174 2691 -266 -238 39 C
ATOM 2795 CG PRO A 356 60.050 53.470 58.632 1.00 19.80 C
ANISOU 2795 CG PRO A 356 2262 2353 2907 -259 -277 50 C
ATOM 2796 CD PRO A 356 59.253 52.247 58.736 1.00 17.89 C
ANISOU 2796 CD PRO A 356 2045 2099 2655 -231 -284 47 C
ATOM 2797 N LYS A 357 56.313 55.526 57.124 1.00 13.28 N
ANISOU 2797 N LYS A 357 1573 1539 1932 -179 -164 -17 N
ATOM 2798 CA LYS A 357 55.413 55.751 56.021 1.00 13.18 C
ANISOU 2798 CA LYS A 357 1569 1544 1894 -128 -130 -41 C
ATOM 2799 C LYS A 357 56.122 55.607 54.651 1.00 12.41 C
ANISOU 2799 C LYS A 357 1449 1427 1840 -138 -102 -27 C
ATOM 2800 O LYS A 357 55.484 55.183 53.685 1.00 12.38 O
ANISOU 2800 O LYS A 357 1429 1443 1833 -106 -72 -39 O
ATOM 2801 CB LYS A 357 54.683 57.067 56.134 1.00 14.28 C
ANISOU 2801 CB LYS A 357 1786 1674 1966 -76 -142 -73 C
ATOM 2802 CG LYS A 357 55.509 58.317 56.081 1.00 15.52 C
ANISOU 2802 CG LYS A 357 2034 1754 2110 -101 -170 -61 C
ATOM 2803 CD LYS A 357 54.580 59.520 56.343 1.00 17.52 C
ANISOU 2803 CD LYS A 357 2395 1985 2277 -19 -201 -103 C
ATOM 2804 CE LYS A 357 55.322 60.840 56.153 1.00 19.65 C
ANISOU 2804 CE LYS A 357 2805 2152 2509 -54 -241 -89 C
ATOM 2805 NZ LYS A 357 56.359 60.969 57.211 1.00 20.96 N
ANISOU 2805 NZ LYS A 357 2979 2293 2692 -147 -267 -56 N
ATOM 2806 N GLU A 358 57.423 55.922 54.540 1.00 12.78 N
ANISOU 2806 N GLU A 358 1486 1451 1919 -188 -110 -6 N
ATOM 2807 CA AGLU A 358 58.053 55.805 53.232 0.60 12.74 C
ANISOU 2807 CA AGLU A 358 1448 1453 1939 -204 -76 -2 C
ATOM 2808 CA BGLU A 358 58.151 55.771 53.262 0.40 13.21 C
ANISOU 2808 CA BGLU A 358 1502 1514 2001 -208 -77 0 C
ATOM 2809 C GLU A 358 58.212 54.317 52.840 1.00 12.84 C
ANISOU 2809 C GLU A 358 1381 1498 2000 -174 -58 -4 C
ATOM 2810 O GLU A 358 58.218 54.000 51.645 1.00 12.66 O
ANISOU 2810 O GLU A 358 1339 1486 1986 -160 -21 -12 O
ATOM 2811 CB AGLU A 358 59.371 56.602 53.162 0.60 13.55 C
ANISOU 2811 CB AGLU A 358 1550 1557 2040 -286 -84 14 C
ATOM 2812 CB BGLU A 358 59.587 56.320 53.371 0.40 14.40 C
ANISOU 2812 CB BGLU A 358 1631 1677 2162 -286 -88 16 C
ATOM 2813 CG AGLU A 358 60.483 56.155 54.093 0.60 13.83 C
ANISOU 2813 CG AGLU A 358 1511 1631 2113 -321 -114 26 C
ATOM 2814 CG BGLU A 358 60.476 55.634 54.400 0.40 15.23 C
ANISOU 2814 CG BGLU A 358 1662 1816 2309 -298 -122 25 C
ATOM 2815 CD AGLU A 358 60.333 56.620 55.561 0.60 13.79 C
ANISOU 2815 CD AGLU A 358 1559 1593 2087 -337 -164 37 C
ATOM 2816 CD BGLU A 358 61.295 54.501 53.827 0.40 15.94 C
ANISOU 2816 CD BGLU A 358 1644 1965 2449 -269 -108 14 C
ATOM 2817 OE1AGLU A 358 59.304 57.247 55.998 0.60 13.39 O
ANISOU 2817 OE1AGLU A 358 1600 1497 1989 -309 -175 28 O
ATOM 2818 OE1BGLU A 358 61.228 54.255 52.593 0.40 16.10 O
ANISOU 2818 OE1BGLU A 358 1641 2003 2472 -251 -63 1 O
ATOM 2819 OE2AGLU A 358 61.304 56.359 56.310 0.60 14.33 O
ANISOU 2819 OE2AGLU A 358 1573 1692 2180 -371 -197 48 O
ATOM 2820 OE2BGLU A 358 62.009 53.851 54.619 0.40 17.29 O
ANISOU 2820 OE2BGLU A 358 1758 2161 2648 -253 -149 15 O
ATOM 2821 N ARG A 359 58.322 53.431 53.816 1.00 12.97 N
ANISOU 2821 N ARG A 359 1373 1518 2035 -165 -91 2 N
ATOM 2822 CA ARG A 359 58.351 52.020 53.509 1.00 13.57 C
ANISOU 2822 CA ARG A 359 1421 1599 2137 -130 -93 -2 C
ATOM 2823 C ARG A 359 56.990 51.525 53.063 1.00 12.33 C
ANISOU 2823 C ARG A 359 1300 1440 1945 -115 -71 -10 C
ATOM 2824 O ARG A 359 56.884 50.723 52.135 1.00 11.52 O
ANISOU 2824 O ARG A 359 1192 1336 1850 -92 -51 -17 O
ATOM 2825 CB ARG A 359 58.831 51.156 54.686 1.00 16.64 C
ANISOU 2825 CB ARG A 359 1810 1974 2541 -126 -152 8 C
ATOM 2826 CG ARG A 359 60.329 51.305 55.020 1.00 20.90 C
ANISOU 2826 CG ARG A 359 2285 2537 3118 -124 -183 8 C
ATOM 2827 CD ARG A 359 61.214 51.212 53.778 1.00 24.29 C
ANISOU 2827 CD ARG A 359 2638 3018 3575 -96 -147 -13 C
ATOM 2828 NE ARG A 359 62.648 51.317 54.070 1.00 31.77 N
ANISOU 2828 NE ARG A 359 3495 4032 4546 -96 -174 -24 N
ATOM 2829 CZ ARG A 359 63.592 51.516 53.148 1.00 31.90 C
ANISOU 2829 CZ ARG A 359 3415 4135 4568 -99 -139 -49 C
ATOM 2830 NH1 ARG A 359 64.884 51.551 53.512 1.00 32.33 N
ANISOU 2830 NH1 ARG A 359 3366 4283 4633 -100 -168 -67 N
ATOM 2831 NH2 ARG A 359 63.265 51.665 51.870 1.00 32.93 N
ANISOU 2831 NH2 ARG A 359 3547 4276 4687 -106 -74 -60 N
ATOM 2832 N LEU A 360 55.947 52.048 53.689 1.00 11.58 N
ANISOU 2832 N LEU A 360 1237 1361 1802 -128 -74 -16 N
ATOM 2833 CA LEU A 360 54.606 51.715 53.236 1.00 11.29 C
ANISOU 2833 CA LEU A 360 1212 1360 1717 -121 -51 -31 C
ATOM 2834 C LEU A 360 54.347 52.252 51.838 1.00 11.21 C
ANISOU 2834 C LEU A 360 1200 1354 1707 -88 -12 -44 C
ATOM 2835 O LEU A 360 53.736 51.582 51.021 1.00 10.40 O
ANISOU 2835 O LEU A 360 1093 1269 1590 -83 8 -51 O
ATOM 2836 CB LEU A 360 53.616 52.225 54.216 1.00 11.93 C
ANISOU 2836 CB LEU A 360 1304 1491 1737 -130 -61 -49 C
ATOM 2837 CG LEU A 360 53.602 51.638 55.614 1.00 12.39 C
ANISOU 2837 CG LEU A 360 1375 1558 1773 -182 -96 -38 C
ATOM 2838 CD1 LEU A 360 52.675 52.497 56.498 1.00 14.14 C
ANISOU 2838 CD1 LEU A 360 1598 1848 1927 -177 -96 -68 C
ATOM 2839 CD2 LEU A 360 53.220 50.176 55.670 1.00 14.02 C
ANISOU 2839 CD2 LEU A 360 1602 1772 1954 -236 -108 -25 C
ATOM 2840 N LYS A 361 54.850 53.447 51.568 1.00 10.93 N
ANISOU 2840 N LYS A 361 1183 1293 1676 -78 -9 -45 N
ATOM 2841 CA LYS A 361 54.746 54.018 50.234 1.00 10.56 C
ANISOU 2841 CA LYS A 361 1159 1233 1620 -60 19 -53 C
ATOM 2842 C LYS A 361 55.417 53.145 49.174 1.00 10.86 C
ANISOU 2842 C LYS A 361 1160 1267 1698 -70 51 -46 C
ATOM 2843 O LYS A 361 54.876 52.929 48.134 1.00 10.43 O
ANISOU 2843 O LYS A 361 1115 1218 1630 -53 76 -54 O
ATOM 2844 CB LYS A 361 55.300 55.449 50.201 1.00 10.63 C
ANISOU 2844 CB LYS A 361 1229 1200 1610 -75 5 -49 C
ATOM 2845 CG LYS A 361 55.098 56.097 48.820 1.00 11.19 C
ANISOU 2845 CG LYS A 361 1356 1243 1651 -66 24 -56 C
ATOM 2846 CD LYS A 361 55.453 57.574 48.856 1.00 11.24 C
ANISOU 2846 CD LYS A 361 1472 1189 1609 -92 -8 -51 C
ATOM 2847 CE LYS A 361 55.072 58.224 47.526 1.00 11.16 C
ANISOU 2847 CE LYS A 361 1552 1139 1551 -79 -5 -58 C
ATOM 2848 NZ LYS A 361 55.597 59.596 47.422 1.00 11.90 N
ANISOU 2848 NZ LYS A 361 1788 1153 1583 -133 -42 -46 N
ATOM 2849 N GLU A 362 56.601 52.632 49.485 1.00 11.03 N
ANISOU 2849 N GLU A 362 1139 1287 1765 -88 45 -36 N
ATOM 2850 CA AGLU A 362 57.267 51.718 48.589 0.50 11.99 C
ANISOU 2850 CA AGLU A 362 1220 1418 1917 -72 69 -43 C
ATOM 2851 CA BGLU A 362 57.277 51.708 48.591 0.50 11.75 C
ANISOU 2851 CA BGLU A 362 1190 1388 1888 -72 69 -43 C
ATOM 2852 C GLU A 362 56.427 50.467 48.314 1.00 11.47 C
ANISOU 2852 C GLU A 362 1176 1342 1841 -44 67 -47 C
ATOM 2853 O GLU A 362 56.360 49.989 47.194 1.00 10.84 O
ANISOU 2853 O GLU A 362 1099 1260 1760 -27 97 -57 O
ATOM 2854 CB AGLU A 362 58.639 51.360 49.150 0.50 13.58 C
ANISOU 2854 CB AGLU A 362 1361 1641 2159 -70 48 -44 C
ATOM 2855 CB BGLU A 362 58.620 51.286 49.179 0.50 12.84 C
ANISOU 2855 CB BGLU A 362 1268 1545 2065 -68 46 -44 C
ATOM 2856 CG AGLU A 362 59.602 52.504 48.970 0.50 16.46 C
ANISOU 2856 CG AGLU A 362 1695 2039 2520 -126 64 -42 C
ATOM 2857 CG BGLU A 362 59.647 52.385 49.206 0.50 14.85 C
ANISOU 2857 CG BGLU A 362 1487 1835 2321 -121 54 -41 C
ATOM 2858 CD AGLU A 362 60.979 52.225 49.525 0.50 18.64 C
ANISOU 2858 CD AGLU A 362 1885 2372 2827 -128 41 -51 C
ATOM 2859 CD BGLU A 362 60.422 52.544 47.902 0.50 16.16 C
ANISOU 2859 CD BGLU A 362 1605 2052 2483 -143 105 -59 C
ATOM 2860 OE1AGLU A 362 61.114 51.437 50.499 0.50 23.09 O
ANISOU 2860 OE1AGLU A 362 2437 2923 3413 -84 -8 -50 O
ATOM 2861 OE1BGLU A 362 60.058 51.913 46.869 0.50 17.08 O
ANISOU 2861 OE1BGLU A 362 1726 2165 2598 -105 138 -73 O
ATOM 2862 OE2AGLU A 362 61.927 52.818 48.993 0.50 21.77 O
ANISOU 2862 OE2AGLU A 362 2225 2834 3212 -182 69 -60 O
ATOM 2863 OE2BGLU A 362 61.427 53.280 47.942 0.50 18.15 O
ANISOU 2863 OE2BGLU A 362 1815 2358 2725 -210 112 -59 O
ATOM 2864 N LEU A 363 55.805 49.915 49.356 1.00 10.72 N
ANISOU 2864 N LEU A 363 1105 1241 1727 -55 30 -39 N
ATOM 2865 CA LEU A 363 54.900 48.761 49.159 1.00 10.39 C
ANISOU 2865 CA LEU A 363 1105 1193 1649 -65 23 -39 C
ATOM 2866 C LEU A 363 53.701 49.091 48.292 1.00 10.27 C
ANISOU 2866 C LEU A 363 1096 1214 1590 -74 56 -49 C
ATOM 2867 O LEU A 363 53.297 48.277 47.499 1.00 10.12 O
ANISOU 2867 O LEU A 363 1103 1190 1553 -80 67 -51 O
ATOM 2868 CB LEU A 363 54.482 48.149 50.498 1.00 10.53 C
ANISOU 2868 CB LEU A 363 1159 1208 1634 -107 -25 -26 C
ATOM 2869 CG LEU A 363 55.613 47.503 51.286 1.00 11.12 C
ANISOU 2869 CG LEU A 363 1251 1233 1743 -86 -77 -17 C
ATOM 2870 CD1 LEU A 363 55.192 47.138 52.710 1.00 11.57 C
ANISOU 2870 CD1 LEU A 363 1357 1282 1757 -144 -127 -1 C
ATOM 2871 CD2 LEU A 363 56.080 46.248 50.592 1.00 12.72 C
ANISOU 2871 CD2 LEU A 363 1500 1383 1951 -43 -97 -25 C
ATOM 2872 N ILE A 364 53.130 50.269 48.473 1.00 9.91 N
ANISOU 2872 N ILE A 364 1037 1205 1522 -68 64 -58 N
ATOM 2873 CA ILE A 364 51.993 50.696 47.648 1.00 9.73 C
ANISOU 2873 CA ILE A 364 1016 1228 1453 -52 83 -76 C
ATOM 2874 C ILE A 364 52.501 50.849 46.185 1.00 9.80 C
ANISOU 2874 C ILE A 364 1040 1198 1487 -32 115 -75 C
ATOM 2875 O ILE A 364 51.853 50.444 45.245 1.00 10.19 O
ANISOU 2875 O ILE A 364 1099 1261 1511 -31 131 -82 O
ATOM 2876 CB ILE A 364 51.412 52.048 48.174 1.00 9.39 C
ANISOU 2876 CB ILE A 364 973 1220 1374 -14 69 -97 C
ATOM 2877 CG1 ILE A 364 50.669 51.811 49.501 1.00 9.64 C
ANISOU 2877 CG1 ILE A 364 978 1323 1361 -37 47 -109 C
ATOM 2878 CG2 ILE A 364 50.510 52.701 47.159 1.00 9.61 C
ANISOU 2878 CG2 ILE A 364 1014 1279 1358 36 75 -122 C
ATOM 2879 CD1 ILE A 364 50.413 53.041 50.360 1.00 9.69 C
ANISOU 2879 CD1 ILE A 364 991 1353 1336 10 26 -134 C
ATOM 2880 N PHE A 365 53.682 51.437 45.992 1.00 10.09 N
ANISOU 2880 N PHE A 365 1075 1194 1563 -29 126 -68 N
ATOM 2881 CA PHE A 365 54.300 51.536 44.673 1.00 10.25 C
ANISOU 2881 CA PHE A 365 1104 1195 1597 -31 163 -70 C
ATOM 2882 C PHE A 365 54.473 50.134 44.033 1.00 10.35 C
ANISOU 2882 C PHE A 365 1106 1202 1624 -23 180 -74 C
ATOM 2883 O PHE A 365 54.083 49.942 42.886 1.00 10.98 O
ANISOU 2883 O PHE A 365 1208 1279 1684 -20 206 -81 O
ATOM 2884 CB PHE A 365 55.623 52.276 44.788 1.00 11.16 C
ANISOU 2884 CB PHE A 365 1202 1300 1737 -58 171 -65 C
ATOM 2885 CG PHE A 365 56.180 52.762 43.473 1.00 11.55 C
ANISOU 2885 CG PHE A 365 1267 1347 1773 -88 211 -69 C
ATOM 2886 CD1 PHE A 365 55.662 53.896 42.898 1.00 12.00 C
ANISOU 2886 CD1 PHE A 365 1404 1375 1781 -104 205 -65 C
ATOM 2887 CD2 PHE A 365 57.282 52.177 42.875 1.00 13.38 C
ANISOU 2887 CD2 PHE A 365 1442 1613 2029 -100 248 -81 C
ATOM 2888 CE1 PHE A 365 56.156 54.391 41.719 1.00 12.65 C
ANISOU 2888 CE1 PHE A 365 1523 1448 1835 -153 237 -64 C
ATOM 2889 CE2 PHE A 365 57.783 52.665 41.645 1.00 13.43 C
ANISOU 2889 CE2 PHE A 365 1460 1636 2007 -148 292 -88 C
ATOM 2890 CZ PHE A 365 57.244 53.802 41.122 1.00 13.60 C
ANISOU 2890 CZ PHE A 365 1576 1616 1977 -188 286 -74 C
ATOM 2891 N GLN A 366 54.979 49.152 44.781 1.00 10.49 N
ANISOU 2891 N GLN A 366 1111 1209 1667 -14 156 -72 N
ATOM 2892 CA GLN A 366 55.156 47.787 44.266 1.00 11.96 C
ANISOU 2892 CA GLN A 366 1324 1369 1853 10 154 -81 C
ATOM 2893 C GLN A 366 53.820 47.141 43.911 1.00 11.44 C
ANISOU 2893 C GLN A 366 1314 1301 1734 -21 147 -75 C
ATOM 2894 O GLN A 366 53.651 46.598 42.822 1.00 11.76 O
ANISOU 2894 O GLN A 366 1386 1325 1757 -15 168 -83 O
ATOM 2895 CB GLN A 366 55.789 46.916 45.337 1.00 13.96 C
ANISOU 2895 CB GLN A 366 1586 1595 2124 33 103 -80 C
ATOM 2896 CG GLN A 366 57.193 47.261 45.690 1.00 17.16 C
ANISOU 2896 CG GLN A 366 1923 2021 2576 71 100 -93 C
ATOM 2897 CD GLN A 366 58.054 47.005 44.578 1.00 20.87 C
ANISOU 2897 CD GLN A 366 2356 2514 3059 118 136 -124 C
ATOM 2898 OE1 GLN A 366 58.718 47.896 44.044 1.00 26.03 O
ANISOU 2898 OE1 GLN A 366 2943 3223 3723 99 181 -135 O
ATOM 2899 NE2 GLN A 366 58.028 45.740 44.139 1.00 21.93 N
ANISOU 2899 NE2 GLN A 366 2547 2607 3178 174 117 -142 N
ATOM 2900 N GLU A 367 52.862 47.217 44.818 1.00 11.13 N
ANISOU 2900 N GLU A 367 1280 1291 1657 -64 120 -64 N
ATOM 2901 CA GLU A 367 51.560 46.554 44.588 1.00 12.22 C
ANISOU 2901 CA GLU A 367 1456 1462 1727 -119 112 -62 C
ATOM 2902 C GLU A 367 50.819 47.106 43.399 1.00 12.52 C
ANISOU 2902 C GLU A 367 1478 1538 1740 -112 145 -73 C
ATOM 2903 O GLU A 367 50.132 46.326 42.663 1.00 13.35 O
ANISOU 2903 O GLU A 367 1623 1652 1799 -149 146 -72 O
ATOM 2904 CB GLU A 367 50.690 46.713 45.844 1.00 13.18 C
ANISOU 2904 CB GLU A 367 1557 1650 1800 -174 85 -58 C
ATOM 2905 CG GLU A 367 51.117 45.843 46.999 1.00 14.16 C
ANISOU 2905 CG GLU A 367 1731 1731 1918 -213 40 -41 C
ATOM 2906 CD GLU A 367 50.621 44.404 46.924 1.00 14.12 C
ANISOU 2906 CD GLU A 367 1826 1695 1843 -293 7 -27 C
ATOM 2907 OE1 GLU A 367 49.514 44.129 46.327 1.00 15.76 O
ANISOU 2907 OE1 GLU A 367 2041 1966 1981 -360 21 -30 O
ATOM 2908 OE2 GLU A 367 51.240 43.525 47.535 1.00 13.61 O
ANISOU 2908 OE2 GLU A 367 1846 1548 1775 -301 -42 -14 O
ATOM 2909 N THR A 368 51.023 48.387 43.130 1.00 11.17 N
ANISOU 2909 N THR A 368 1273 1379 1593 -68 163 -82 N
ATOM 2910 CA THR A 368 50.348 49.046 42.014 1.00 11.48 C
ANISOU 2910 CA THR A 368 1316 1442 1602 -49 181 -93 C
ATOM 2911 C THR A 368 51.132 48.919 40.705 1.00 11.51 C
ANISOU 2911 C THR A 368 1352 1389 1632 -37 216 -92 C
ATOM 2912 O THR A 368 50.645 49.344 39.663 1.00 11.34 O
ANISOU 2912 O THR A 368 1353 1374 1583 -29 228 -98 O
ATOM 2913 CB THR A 368 50.057 50.515 42.322 1.00 11.39 C
ANISOU 2913 CB THR A 368 1292 1456 1579 -4 166 -107 C
ATOM 2914 OG1 THR A 368 51.261 51.227 42.618 1.00 10.70 O
ANISOU 2914 OG1 THR A 368 1215 1311 1538 5 172 -97 O
ATOM 2915 CG2 THR A 368 49.131 50.617 43.530 1.00 12.15 C
ANISOU 2915 CG2 THR A 368 1346 1636 1634 -5 136 -121 C
ATOM 2916 N ALA A 369 52.358 48.395 40.727 1.00 11.42 N
ANISOU 2916 N ALA A 369 1340 1334 1667 -29 232 -91 N
ATOM 2917 CA ALA A 369 53.196 48.380 39.567 1.00 11.45 C
ANISOU 2917 CA ALA A 369 1352 1313 1686 -17 273 -101 C
ATOM 2918 C ALA A 369 52.598 47.596 38.402 1.00 12.38 C
ANISOU 2918 C ALA A 369 1519 1418 1767 -24 288 -106 C
ATOM 2919 O ALA A 369 52.790 47.936 37.257 1.00 12.26 O
ANISOU 2919 O ALA A 369 1521 1396 1741 -26 323 -114 O
ATOM 2920 CB ALA A 369 54.559 47.820 39.955 1.00 12.28 C
ANISOU 2920 CB ALA A 369 1424 1407 1835 12 279 -112 C
ATOM 2921 N ARG A 370 51.838 46.565 38.667 1.00 12.58 N
ANISOU 2921 N ARG A 370 1579 1440 1762 -46 259 -100 N
ATOM 2922 CA AARG A 370 51.439 45.733 37.546 0.50 13.32 C
ANISOU 2922 CA AARG A 370 1734 1510 1816 -61 271 -105 C
ATOM 2923 CA BARG A 370 51.354 45.682 37.612 0.50 13.68 C
ANISOU 2923 CA BARG A 370 1781 1557 1858 -64 267 -104 C
ATOM 2924 C ARG A 370 50.324 46.343 36.708 1.00 12.96 C
ANISOU 2924 C ARG A 370 1693 1506 1726 -87 276 -102 C
ATOM 2925 O ARG A 370 50.034 45.845 35.663 1.00 13.84 O
ANISOU 2925 O ARG A 370 1854 1601 1806 -102 289 -105 O
ATOM 2926 CB AARG A 370 51.116 44.333 37.976 0.50 14.34 C
ANISOU 2926 CB AARG A 370 1933 1605 1909 -92 231 -98 C
ATOM 2927 CB BARG A 370 50.770 44.407 38.219 0.50 15.18 C
ANISOU 2927 CB BARG A 370 2032 1730 2005 -111 222 -93 C
ATOM 2928 CG AARG A 370 49.886 44.188 38.816 0.50 14.54 C
ANISOU 2928 CG AARG A 370 1956 1687 1881 -169 193 -80 C
ATOM 2929 CG BARG A 370 49.500 44.605 39.001 0.50 16.21 C
ANISOU 2929 CG BARG A 370 2135 1938 2085 -179 192 -79 C
ATOM 2930 CD AARG A 370 49.611 42.715 38.869 0.50 15.64 C
ANISOU 2930 CD AARG A 370 2208 1774 1960 -228 154 -71 C
ATOM 2931 CD BARG A 370 49.229 43.429 39.925 0.50 17.32 C
ANISOU 2931 CD BARG A 370 2343 2060 2179 -249 145 -65 C
ATOM 2932 NE AARG A 370 48.550 42.278 39.793 0.50 16.09 N
ANISOU 2932 NE AARG A 370 2282 1889 1942 -340 113 -52 N
ATOM 2933 NE BARG A 370 49.760 43.766 41.246 0.50 18.52 N
ANISOU 2933 NE BARG A 370 2455 2213 2370 -229 126 -61 N
ATOM 2934 CZ AARG A 370 48.725 42.138 41.111 0.50 16.46 C
ANISOU 2934 CZ AARG A 370 2329 1935 1989 -364 80 -42 C
ATOM 2935 CZ BARG A 370 49.490 43.142 42.383 0.50 18.49 C
ANISOU 2935 CZ BARG A 370 2490 2211 2326 -296 82 -46 C
ATOM 2936 NH1AARG A 370 47.744 41.685 41.895 0.50 16.54 N
ANISOU 2936 NH1AARG A 370 2361 2011 1912 -489 47 -28 N
ATOM 2937 NH1BARG A 370 50.057 43.608 43.502 0.50 15.86 N
ANISOU 2937 NH1BARG A 370 2114 1878 2035 -266 69 -44 N
ATOM 2938 NH2AARG A 370 49.900 42.454 41.639 0.50 16.90 N
ANISOU 2938 NH2AARG A 370 2361 1935 2123 -273 80 -49 N
ATOM 2939 NH2BARG A 370 48.632 42.107 42.418 0.50 20.02 N
ANISOU 2939 NH2BARG A 370 2771 2411 2424 -408 50 -32 N
ATOM 2940 N PHE A 371 49.755 47.467 37.170 1.00 12.33 N
ANISOU 2940 N PHE A 371 1567 1477 1639 -78 260 -101 N
ATOM 2941 CA PHE A 371 48.844 48.292 36.365 1.00 12.09 C
ANISOU 2941 CA PHE A 371 1543 1483 1566 -67 253 -108 C
ATOM 2942 C PHE A 371 49.525 49.412 35.574 1.00 13.74 C
ANISOU 2942 C PHE A 371 1784 1646 1790 -38 274 -110 C
ATOM 2943 O PHE A 371 48.879 50.133 34.819 1.00 13.57 O
ANISOU 2943 O PHE A 371 1797 1632 1727 -20 257 -115 O
ATOM 2944 CB PHE A 371 47.709 48.854 37.234 1.00 11.92 C
ANISOU 2944 CB PHE A 371 1468 1554 1505 -52 210 -119 C
ATOM 2945 CG PHE A 371 46.908 47.820 37.907 1.00 12.41 C
ANISOU 2945 CG PHE A 371 1501 1688 1525 -115 192 -118 C
ATOM 2946 CD1 PHE A 371 45.790 47.231 37.306 1.00 12.65 C
ANISOU 2946 CD1 PHE A 371 1530 1793 1484 -166 179 -123 C
ATOM 2947 CD2 PHE A 371 47.271 47.394 39.137 1.00 13.51 C
ANISOU 2947 CD2 PHE A 371 1623 1825 1683 -142 184 -109 C
ATOM 2948 CE1 PHE A 371 45.046 46.252 37.988 1.00 13.90 C
ANISOU 2948 CE1 PHE A 371 1671 2030 1582 -261 160 -119 C
ATOM 2949 CE2 PHE A 371 46.570 46.415 39.787 1.00 14.98 C
ANISOU 2949 CE2 PHE A 371 1807 2073 1814 -227 163 -104 C
ATOM 2950 CZ PHE A 371 45.448 45.843 39.208 1.00 14.39 C
ANISOU 2950 CZ PHE A 371 1732 2078 1658 -296 152 -108 C
ATOM 2951 N GLN A 372 50.846 49.560 35.721 1.00 14.55 N
ANISOU 2951 N GLN A 372 1882 1708 1940 -41 306 -107 N
ATOM 2952 CA GLN A 372 51.614 50.500 34.921 1.00 16.03 C
ANISOU 2952 CA GLN A 372 2106 1862 2123 -55 333 -107 C
ATOM 2953 C GLN A 372 51.876 49.935 33.521 1.00 19.29 C
ANISOU 2953 C GLN A 372 2557 2256 2515 -78 377 -115 C
ATOM 2954 O GLN A 372 51.932 48.732 33.304 1.00 20.08 O
ANISOU 2954 O GLN A 372 2650 2356 2623 -74 394 -123 O
ATOM 2955 CB GLN A 372 52.976 50.768 35.544 1.00 15.29 C
ANISOU 2955 CB GLN A 372 1970 1766 2071 -71 358 -108 C
ATOM 2956 CG GLN A 372 52.966 51.546 36.821 1.00 14.96 C
ANISOU 2956 CG GLN A 372 1909 1730 2044 -60 320 -99 C
ATOM 2957 CD GLN A 372 52.526 52.971 36.622 1.00 14.88 C
ANISOU 2957 CD GLN A 372 1977 1691 1987 -60 285 -94 C
ATOM 2958 OE1 GLN A 372 53.204 53.748 35.942 1.00 16.42 O
ANISOU 2958 OE1 GLN A 372 2230 1853 2154 -112 301 -88 O
ATOM 2959 NE2 GLN A 372 51.370 53.353 37.233 1.00 13.52 N
ANISOU 2959 NE2 GLN A 372 1814 1533 1790 -3 230 -101 N
ATOM 2960 N PRO A 373 52.139 50.814 32.566 1.00 22.20 N
ANISOU 2960 N PRO A 373 2984 2602 2849 -109 394 -113 N
ATOM 2961 CA PRO A 373 52.098 52.263 32.686 1.00 25.03 C
ANISOU 2961 CA PRO A 373 3399 2933 3177 -122 361 -102 C
ATOM 2962 C PRO A 373 50.672 52.711 32.431 1.00 27.56 C
ANISOU 2962 C PRO A 373 3776 3245 3449 -72 297 -102 C
ATOM 2963 O PRO A 373 49.845 51.889 32.121 1.00 30.21 O
ANISOU 2963 O PRO A 373 4089 3612 3776 -52 292 -108 O
ATOM 2964 CB PRO A 373 53.003 52.711 31.544 1.00 25.28 C
ANISOU 2964 CB PRO A 373 3489 2945 3172 -198 409 -101 C
ATOM 2965 CG PRO A 373 52.786 51.653 30.531 1.00 22.80 C
ANISOU 2965 CG PRO A 373 3173 2641 2850 -195 446 -114 C
ATOM 2966 CD PRO A 373 52.767 50.394 31.303 1.00 22.94 C
ANISOU 2966 CD PRO A 373 3104 2689 2923 -146 451 -125 C
ATOM 2967 N GLY A 374 50.415 54.008 32.459 1.00 30.93 N
ANISOU 2967 N GLY A 374 4289 3632 3832 -52 245 -99 N
ATOM 2968 CA GLY A 374 49.076 54.524 32.084 1.00 38.46 C
ANISOU 2968 CA GLY A 374 5302 4585 4726 24 172 -111 C
ATOM 2969 C GLY A 374 48.952 54.846 30.589 1.00 41.74 C
ANISOU 2969 C GLY A 374 5834 4946 5080 -6 166 -105 C
ATOM 2970 O GLY A 374 48.055 54.333 29.888 1.00 47.78 O
ANISOU 2970 O GLY A 374 6593 5742 5820 22 151 -114 O
TER 2971 GLY A 374
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